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14 Biological Chemistry Part (ii)Enzyme Chemistry By C. A. ROSS Department of Biochemistry University College Cork Lee Makings Prospect Row Cork Ireland 1 Introduction In stark contrast to recent times the past year has seen very little activity by writers of texts on enzymology. There has been the appearance of one book,’ which is cast in much the same mould as Foster’s ‘The Nature of Enzymology’. It succeeds well at the level of introductory university courses but poor diagrams and typesetting detract from its appearance. From Academic Press come two new series. One is entitled ‘Benchmark Papers in Biochemistry’ the first volume of which is devoted to enzymes.’ Here is a chance to read in English original papers by many of the pioneer workers in the field some of whom have tended to be overlooked by modern authors.Oddly enough that most quoted of papers by Lineweaver and Burk3 is not included. The other new series is entitled ‘Selected Methods in Enzymology’. Such has been the rapid advance of the subject matter and the technology of biochemistry since 1955 when the first of the four original volumes of ‘Methods in Enzymology’ appeared as a compendium of available techniques that the original series has run to over sixty volumes with a bewildering sequence of titles. It has now been decided to produce single volumes in selected areas that will contain basic methodology. The first of these volumes4 is significantly devoted to RNA and protein synthesis. It has of course been apparent for some years past that the main growth area in biochemistry has been in the area of molecular biology.Following the discovery of the double helical structure of DNA and subsequently the nature of the genetic code in the 1960’s a lull ensued which has ended with the ability to sequence DNA and to manipulate genetic material. The importance that this work holds is highlighted by the Nobel Awards in chemistry and in medicine or physiology in recent years. F. Sanger achieved a most notable success in being awarded in 1980 a second Nobel Prize in chemistry and his Lecture has now appeared in print’” as have those of P. Berg” and W. Gilbert.” This report begins with a short review of the chemistry of the enzymes that are the very basis of this new area. For biochemistry the 1980’s will see enormous strides in the field of T.Palmer ‘Understanding Enzymes’ Ellis Horwood Ltd. Chichester 1981. ’Benchmark Papers in Biochemistry Vol. 1 Enzymes’ ed. H. C. Friedman Academic Press New York 1981. H. Lineweaver and D. Burk J. Am. Chem. Soc. 1934,56,658. ‘RNA and Protein Synthesis’ ed. K. Moldave Academic Press New York 1981. ’ (a)F. Sanger Biosc. Rep. 1981.1 3; (b)P. Berg ibid. p. 269; (c) W.Gilbert ibid.,p. 353. 381 382 C. A. Ross molecular genetics with all its attendant moral and ethical problems. With the passing of the era of metabolic biochemistry it is poignant to record too the passing of Sir Hans Krebs at the age of 81. He had made that era his own. 2 Restriction Endonucleases Bacteria are capable of destroying foreign DNA by splitting the double-stranded polynucleotide at a limited number of sites.This ability resides in strain-specific restriction endonucleases. At the same time the DNA of the host cell is protected against its own enzymes by methylation of adenine and cytosine residues at the specific sites recognized by the restriction enzymes. Originally it was thought that the restriction site and the methylation site were one and the same for a particular restriction and modifying (methylating) enzyme but this is now known to be not necessarily true. Sufficient numbers of restriction endonucleases have been detected and characterized to enable at least three classes to be identified and the basis of the classification can best be summarized in table form.From Table 1 it can be Table 1 Characteristics of restriction endonucleases (modified from ref. 6) Type I Type 11 Type 111 1. Restriction and modification activities Single multifunctional enzyme Separate endonuclease and methylase Single multifunctional enzyme 2. Protein structure 3 different subunits Simple 2 different subunits 3. Requirements for restriction ATP.Mg2+ SAM Mg" ATP.Mg2' (SAM) 4. Sequence of host specificity sites' sB:T-G-A-Ng-T-sK:A-A-C-N6-G-C-T Two-fold symmetry SP1 A-G-A-C-C ~1.5 C-A-G-C- A-G G-T-G-C 5. Cleavage sites Possibly random at least 1000 bp from host specificity site Generally at host specificity site 24-26 bp to 3' of host specificity site 6. Requirements for me thylation (ATP.Mg2+) SAM SAM (ATP.Mg2+) SAM 7. Restriction us.methylation Mutually exclusive Separate reactions Simultaneous 8. Site of methylation Host specificity site Host specificity site Host specificity site The host specificity sites sB sK sP1 and s15 refer to E. coli B E. coli K phage PI and plasmid P1S. Type I enzymes have a hyphenated site with two constant domains of 3 and 4 bases separated by a nonspecified spacer of 6 or 8 bases (Reproduced with permission from Annu. Rev. Biochem. 1981 50 285) seen that type I and type I11 endonucleases are multimeric multifunctional enzymes that require ATP S-adenosyl methionine (SAM) and Mg2+ as factors or activators of the cleavage and modifying activities. Furthermore type I enzymes are powerful ATPases. Both types have recently been reviewed.6 Whereas types I and I11 enzymes cleave the polynucleotide chain at a point distant from the specificity site (in itself ' R.Yuan Annu. Rev. Biochem. 1981,50 285. Biological Chemistry -Part (ii) Enzyme Chemistry a remarkable phenomenon) type I1 endonucleases usually cleave and methylate at the same site. They have the simplest protein structure and minimal requirements for both restriction (nucleolytic cleavage) and methylation. The detailed study of the type I1 has focused primarily on the Eco RI enzyme.'* At this point a short explanation is required of the notation used for the naming of restriction enzymes due to Smith and Nathans.' An italicized three-letter abbreviation is used for the host organism followed by where necessary a fourth letter for strain and a roman numeral to indicate each RM system in the organism.Thus Hind I1 is the name of an RM system in Haemophilus influenrue strain Rd. Similarly Eco RI describes an enzyme found in Escherichia coli R that has the recognition sequence shown in Scheme 1,where an arrow indicates the point of cleavage and the asterisk 5'-G?A-i-T-T-C-3' 3'-C-T-T-I-A7G-5' indicates centre of two-fold symmetry Scheme 1 the group which is methylated. The availability of enzymes with highly specific and limited sites for cleaving DNA molecules has been immensely valuable in the task of determining nucleotide sequences and they have been described as 'the molecular scalpels of the contemporary biologist'.'" In fact DNA sequencing is faster and more accurate than protein sequencing largely because of the techniques introduced by Sanger.sa.9b This is remarkable since it was considered that DNA sequencing would be extremely difficult if not impossible owing to the nature of the primary structure.Degradation by chemical means or by the nucleases then known led to the produc- tion of large numbers of small oligonucleotides. The discovery of endonucleases with specificities involving sequences of bases that occur relatively rarely in the polynucleotide has served to revolutionize sequence analysis. At a higher level of complexity using techniques employing the same principles it has been possible to construct physical maps of chromosomes in which restriction enzyme cleavage sites serve as defined reference points.Referring to Scheme 1 the two strands of duplex DNA are seen to be cleaved at points that are not opposite each other and so give rise to cohesive ends that hold the strands together by hydrogen bonding until steps are taken to separate them. Originally cohesive ends composed of several bases of one type (e.g. oligo-dA) were added to a polynucleotide chain which would then anneal with a chain to which a short length of complementary base (oligo-dT in this case) had been attached by a polymerase enzyme. However new restriction enzymes are con- tinually being reported and a list compiled annually by Roberts" now contains ' (a)R. D. Wells R. D. Klein and C. K. Singleton in 'The Enzymes Third Ed. Vol. 14 Nucleic Acids Part A' ed. P. D. Boyer Academic Press New York 1981; (b) P.Modrich Quart. Rev. Biophys. 1979 12 315. * H. 0.Smith and D. Nathans J. Mol. Bid 1973,81 419. (a)M. Zabeau and R. J. Roberts in 'Molecular Genetics Part 111' ed. J. H. Taylor Academic Press New York 1979; (b)P.A. Biro and S. Weissman ibid. in (a)R. J. Roberts Nuckic Acid Res. 1981,9 75; (b)Gene 1980 8 329. 384 C.A. Ross over 200 entries. Each enzyme has a different specificity site and/or cleavage site so that it is possible to cleave one DNA molecule to produce a ‘sticky end’ that will anneal with another DNA strand produced by a different restriction enzyme. Covalent joining is then effected by means of a ligase enzyme. The isolation of particular DNA segments by molecular cloning5b involves the insertion of DNA fragments at particular sites in suitable receptor DNA molecules called ‘vectors’ which are capable of replicating autonomously.A large number of these are now available for cloning DNA segments in E. coli. Thus the synthesis of human interferon all and interferon PI,’’ has recently been achieved in E. coli infected by a A phage recombinant containing a human genomic fragment. Such genetic engineering feats hold out the best hope for producing scarce biological materials on a commercial basis. In the field of clinical diagnosis the new technology is proving to be a powerful tool. For example,” DNA from a normal human digested with MbO I1 gives three bands of 1600 580 and 400 base pairs that hybridize with cloned human insulin cDNA probes.DNA from a diabetic patient with a mutant insulin gave an additional band of 980 base pairs on digestion and hybridization. A MbO I1 cleavage site has thus been lost in the mutant. The effect of this on insulin is expressed as a leucine residue being incorporated at either position B-24 or B-25 instead of phenylalanine. 3 Kinetic Analysis The proceedings of a satellite symposium on Design and Analysis of Enzyme and Pharmacokinetic Experiments held in conjunction with the XI International Con- gress of Biochemistry have now been p~blished.’~ There are sections on nonlinear regression robust parameter estimation and the design of experiments kinetic model identification and kinetic data analysis. Further contributions on the statis- tical treatment of kinetic data have been made by Cornish-Bowden and Endrenyi” and by Oppenheimer et ~1.’~ Waley” had produced an easy method for determining initial rates of reactions where the Michaelis-Menten equation is obeyed.Instead of attempting to draw tangents to the progress curve at zero time a chord is drawn between two points on the curve and its slope gives the rate at an intermediate substrate concentration. The value of this intermediate concentration is calculated from relationships derived from the integrated form of the Michaelis-Menten equation. Thus when the concentration of product is being monitored the intermediate concentration of product formed P3 is given by equation (1). (1) S. Nagata N. Mantei and C. Weissmann Name (London) 1980 287,401.Y.Mory er al. Eur. J. Biochem. 1981 120 197. l3 S. C. M. Kwok S. J. Chan A. H. Rubenstein R. Poncher and D. F. Steiner Biochem. Biophys. Res. Commun. 1981.98 844. l4 ‘Kinetic Data Analysis’ ed. L. Endrenyi Plenum Press New York 1981. *5 A. Cornish-Bowden and L. Endrenyi Biochem. J. 1981,193,1005. l6 L.Oppenheimer T. P. Capizzi and G. T. Miwa Biochem. J. 1981,197,721. S. G. Waley Biochem. J. 1981 193 1009. Biological Chemistry -Part (ii) Enzyme Chemistry 385 Only one datum point need be used when the calculation is of course simplified since P1 =0 at zero time. In order to obtain the correct values for Vmaxand K, two chords are required (e.g.one from 0-20°/0 reaction of slope v and the other from 040% reaction of slope v’) in order to calculate the rate vo when the concentration of product is zero.Then So6 -S’) where S and S’are the substrate concentrations corresponding to the rates v and v’.The use of this equation is recommended if the product is a powerful inhibitor. Otherwise a plot of v against p will give an intercept at p =0 equal to the initial rate vo. The ratio of the two slopes v/v’ already mentioned will lie between 1 and 1.145 when there is no product inhibition nor enzyme inactivation. However if there is product inhibition the upper bound of this quotient is approximately 2.2 so that it is possible to detect product inhibition from the results of a single experiment ! A new method has been described for plotting kinetic results for inhibited enzyme reactions18 and consists of plotting data in a normalized fashion.Thus vo/vi the ratio of the initial velocities for the non-inhibited and inhibited reactions is plotted versus the specific velocity r/(l+CT) where CT is the [S]/K ratio. The method provides a simple way of determining the inhibition constants Ki and KI the dissociation constants of the EI and ESI complexes respectively by replots of intercepts of the primary specific velocity plot. The method is applied to two actual examples elastase inhibition by a glycosaminoglycan polysulphate and glycogen phosphorylase inhibition by glucose 6-phosphate. The kinetics of suicide substrates based on the scheme due to Walsh et a/.” (see Scheme 3 in last year’s Report) have been reworked and results more consistent with exact solutions obtained.The most important factor was found to be the term (1 +r)p instead of rp as proposed by Waley where r is the ratio of the rate constant of product formation to that of enzyme inactivation and p is the ratio of initial concentration of enzyme to that of suicide substrate. Continuing his thesis that enzymes do not usually obey the Michaelis-Menten equation Bardsley has published further papers” on the computation of the probabilities of obtaining complex curves from simple kinetic schemes and on the probability that complex kinetic curves can be caused by activators or inhibitors. Considering crude enzyme samples may contain unknown amounts of endogenous substrate reaction product inhibitor and even contaminating enzymes and yet are used to evaluate the kinetic parameters K and V,an interesting novel analytical method has been described.” In the presence of endogenous substrate (concentra- tion x) and contaminating enzyme (activity u),the Michaelis-Menten equation can A.Baici Eur. J. Bioehem. 1981 119 9. 19 S.Tatsunami N Yago and M. Hosoe Biochim. Biophys. Am 1981,662,226. *’ (a)F. Solano-Mufioz P. B. McGuilay R. Woolfson and W. G. Bardsley Eiochem. J. 1981,193,339; (b)F.Solano-Mufioz W. G. Bardsley and K. J. Indge ibid. 1981 195 589. 21 M. G. Kato and N. Inoue Biochim. Biophys. Aefa,1981,661 1. 386 C.A. Ross be rewritten as where vi is an observed reaction rate at a concentration of exogenously added substrate Sl. When substrate is not added (S; = 0) DO = (VX/K + X) + u (4) These equations can be rearranged to give which is of the general form y/b = x/a = 1 representing a straight line in xy space with intercept a on the x axis and intercept b on the y axis.Thus the equation represents a straight line when -Sl is plotted on the x axis as a and (ui -vo)/vo is plotted on the y axis as b (cf. the direct plot of Eisenthal and Cornish-Bowden) as shown in Figure 1.In the case where no contaminating enzyme is present (u = 0))A = (K,+ x) and B = K,/x so that K = AB/(B+ 1)andx = A(B + 1). (6) Where a contaminating enzyme is present (u # O) A = (K,+ x) and B = K,/x(l -u/vo).Two concentration levels of endogenous substrate are used to give two pairs of co-ordinates for the evaluation of the parameters.X a -Si I Figure 1 Linear plot An increasingly important aspect of enzyme kinetics is that in which the reaction occurs between two phases as with insoluble substrates or immobilized enzymes. In such situations the reaction rates are directly related to the area concentration Biological Chemistry -Part (ii)Enzyme Chemistry 387 of bulk solution which is defined as the two thirds power of volume concentration.” Thus for an immobilized enzyme the Michaelis-Menten equation is modified to v[s]2’3 v= KL + [S]’” where KL is the modified Michaelis-Menten constant. In similar fashion the Langmuir adsorption isotherm may also be modified. The modified equations have been tested experimentally and do appear to be obeyed over a greater concentration range than the unmodified expressions.On the subject of immobilized enzyme systems Mosbach the immobilization of the four urea cycle enzymes to the same Sepharose particles resulting in greater catalytic efficiency than the soluble system and operating in a cyclic manner. The same worker also reportsz4 an easy method for activating hydroxy-group-carrying supports with 2,2,2-trifluoroethanesulphonyl chloride resulting in much improved coupling yields (up to 80%) and retained specific activities (up to 50%).An interesting use of immobil- ized enzymes has resulted in the demon~tration’~ of physical interactions between different enzymes of the citric acid cycle and the aspartate-malate shuttle. It is shown that maximally four molecules of malate dehydrogenase bind to one fumarase molecule and that this complex is then able to bind to either citrate synthase or aspartate aminotransferase.The suggestion is that the enzymes bind alternatively in order to allow the cell to perform either cycle or shuttle reactions according to its needs. An intriguing concept that of energy cost of catalytic turnover owing to enzyme degradation in viuo has been explored.26 On the basis that four ATPs are required in the formation of a single peptide bond it is possible to calculate the energy required to make an enzyme molecule. Given the half-life of the enzyme and its turnover number it is then possible to calculate the number of ATPs amortized per catalytic turnover. Data on some twenty rat liver enzymes has been examined in this way and an eight-order-of-magnitude range results.4 pHEffects The variation in enzyme-catalysed reaction rates with pH has always been an obvious line to follow in investigating mechanisms of action. However the interpre- tation of the experimental data is fraught with difficulties. One basic source of error in the pH measurements themselves has been rep~rted.~’ In glass-electrode assem- blies in which the reference half-cell contains a porous ceramic plug errors arise from substantial liquid-junction potentials. The size of the error is proportional to the ratio between the salt concentration in the standard buffers and in the unknown solutions. Although the error varies from one electrode specimen to another the average was found to be 0.2pH unit per 10-fold salt concentration difference between standard and test solutions.The author claims that errors of this order must be widespread in the recent literature since the introduction of this design of electrode. 22 M.-G. Lee and W.-C. Chiang Biochem. Int. 1981,2,1. 23 N.Siegbahn and K. Mosbach FEBSLett. 1982 137 6. 24 K.Nilsson and K. Mosbach Biochem. Biophys. Res. Commun. 1981,102,449. 25 S.Beeckmans and L. Kanarek Eur. J. Biochem. 1981,117 527. 26 M.N. Kazarinoff Arch. Biochem. Biophys. 1981,208 131. 27 J. A.Illingworth Biochem. J. 1981,195,259. 388 C. A. Ross A standard procedure for the analysis of kinetic data for regulatory enzymes as a function of pH has been presented2* using the limiting hyperbolae predicted by the exponential model for a regulatory enzyme VAa0exp kPa v= 1 + Aaoexp kPa where a.is the association-binding constant characterizing the original state of the enzyme k is the interaction free energy and P. is the fractional saturation. Such an expression predicts two limiting hyperbolae as Paapproaches its limiting values of 0 and 1.The relationship between the exponential model parameters k and ao the Hill coefficient h and the substrate concentration at half-saturation So.5,is shown as k = 4(h -l)/h and In a. = -(In So.5+ k/2). (9) Data from the literaturezg on the pH dependence of the reaction catalysed by aspartate transcarbamylase (aspartate carbamoyl-transferase) has been analysed and shows a significant shift in the pK values for the free enzyme as the conforma- tional state of the enzyme varies.These shifts reflect changes in the environment of ionizable groups within the active site. From Cleland's laboratory comes the results of a pH study to elucidate the mechanism of creatine kinase which catalyses the reversible phosphorylation of creatine by MgATPe3' The pH profiles from initial velocity measurements are interpreted as suggesting the presence of a single group with a pK near 7 that acts as an acid-base catalyst and must be unprotonated in the direction of creatine phosphorylation and protonated for Mg-ADP phosphorylation. In addition another group with a pK near 6 must be unprotonated for activity in either direction. Solvent perturbation of apparent pK values allows one to determine whether the groups involved are neutral or cationic acids.Cationic acids such as the nitrogen bases exhibit little change in pK when organic solvent is added since a net positive charge is present before and after dissociation of the acid. Neutral acids such as carboxy-groups on the other hand show an increase in pK since a new positive and negative charge are present after dissociation which is impeded by the presence of the solvent. Since the pK is near 7 the decrease in the apparent pK of the acid-base catalytic group in these experiments is interpreted as indicating that the group is probably histidine but that it is a lysine with a low pK cannot be ruled out. Similarly the group that must be ionized and that has a pK near 6 has been shown to be a carboxylic acid group.The chemical reaction catalysed by creatine kinase may be written in the form -+R-NH2 + MgATP2-$ -+R-NH-PO:-+ MgADP-+ H' (10) where -+R-NH2 represents creatine. Hence an acid-base catalyst such as histidine will accept a proton from the guanidinium group during phosphorylation of creatine and donate a proton during the reverse reaction. It is interesting to note that in other kinases such as hexokinase and fructokinase the acid-base catalyst has been identified as a carboxy-group (as an aspartate in the case of hexokinase3*). Cleland 28 R. B. Gregory and S. Ainsworth Biochim. kiophys. Acta 1981,659,249. 29 S. C. Pastra-Landis D. R. Evans and W. N. Lipscomb J. Eiol. Chem. 1978 253,4624. '' P.F.Cook G.L. Kenyon and W. W. Cleland Eiochemisfry 1981 20 1204. 31 C. M.Anderson R. E. Stenkamp R. C. McDonald and T.A. Steitz J. Mol. Eiol. 1978 123 207. Biological Chemistry -Part (ii) Enzyme Chemistry argues that as creatine kinase catalyses a reaction which must be freely reversible in muscle the acid-base catalyst must have a pK closely matching the pH of the cell i.e. that for a histidine rather than of a carboxy-group. Furthermore the phosphorylation of a positively charged guanidinium group would present difficulties if the NH2 group formed a hydrogen bond with an ionized carboxy-group. The negative charge of the carboxy-group would be likely to attract much of the positive charge of the guanidinium group to the nitrogen and make it a much poorer nucleophile A neutral histidine would not have the same effect.A possible structure of the transition state for phosphoryl transfer is shown in Scheme 2 in which the (Ad = adenosine; E = enzyme) Scheme 2 ionized carboxy-group is depicted interacting with one of the guanidinium nitrogens while the other is shown speculatively as interacting with the carboxy-group of creatine in order to localize the positive charge away from the nitrogen being phosphorylated. The effect of ionic strength on the pK of an essential acidic group on glucose oxidase has been rep~rted.~’ The kinetics of the reaction are easily analysed according to Scheme 3. I dissociation Of an essential Eo’H202 acidic group (G = glucose; P = product) Scheme 3 Analysis of the ionic strength dependence of pK4.0br assuming that the enzyme is an homogeneously charged impenetrable sphere predicts that the intrinsic pK of the acidic group is 6.7.A van’t Hoff plot of the temperature dependence of K4,0br gave values for AHo and AS0 consistent with the group responsible being a histidine residue. J. G.Voet J. Coe 1. Epstein V. Matossian and T.Shipley Biochemistry 1981,20 7182. 390 C.A. Ross 5 Dehydrogenases In a series of papers,33 Cook and Cleland have presented some detailed mechanistic deductions from isotope effects. First from the magnitude of the isotope effects on V and V/K for various substrates using both labelled and unlabelled substrates information can be obtained on the order of addition of reactants as well as on the location and degree of rate limitation of the isotope-sensitive steps.Secondly by making use of the equilibrium perturbation method to determine the effect of reactants other than those involved in the perturbation on the rate of release of the perturbant molecules from the enzyme it has been possible to distinguish between ordered and random binding. Thus for liver alcohol dehydrogenase NAD is not released at an appreciable rate from the E-NAD-cyclohexanol complex whereas cyclohexanol is released much more readily than it reacts to give products so that the mechanism appears ordered. With NADH and cyclohexanone however since NADH is released at a finite rate from the complex the reaction is random. Conversely for the yeast enzyme NADH release from the enzyme is prevented by acetone so giving the appearance of an ordered mechanism whereas the reverse reaction is random since propan-2-01 and NAD are released at equal rates.In order to enhance observed isotope effects and obtain more useful information on the kinetic mechanism the variation of pH on isotope effects has been studied. In the first case where the bond-breaking (i.e. isotope-dependent) step is pH depen- dent the model predicts that; at the optimum pH an increase in the V/K isotope effect shows that the substrate is sticky (i.e. reacts to give products as fast as or faster than it dissociates) whereas an increase in the V isotope effect shows that some other pH-independent step is at least partly limiting.The theory has been verified in the case of three dehydrogenases. In the second case where the isotope- dependent step is not pH-dependent the isotope effects fall to 1.0 in the forward direction and this model accurately describes the kinetics of yeast and liver alcohol dehydrogenases where hydride transfer to an aldehyde or ketone from NADH to give an alkoxide is isotope sensitive but largely pH independent. The subsequent protonation of the alkoxide requires that an enzyme group (possibly His-51 in the liver enzyme) be protonated. In the final paper secondary isotope effects have been employed to investigate the chemical mechanism of liver alcohol 7toHis-51 H R R E-NAD-alcohol E-NAD-alkoxide E-NADH-ketone E-NADH Scheme 4 33 P.F.Cook and W.W. Cleland Biochemistry 1981,20 1790;ibid. p. 1797,ibid. p. 1805,ibid. p. 1817. Biological Chemistry -Part (ii)Enzyme Chemistry 391 dehydrogenase. Secondary isotope effects result from isotopic substitution in atoms that do not undergo cleavage but change the stiffness of their bonding during the reaction. Thus it is claimed that NAD develops carbonium ion character at C-4 as the result of geometric distortion before hydride transfer. In Scheme 4 the E-NAD-alkoxide complex is shown with the sugar-base bond bent out of the plane of the nicotinamide ring so that N-1 is no longer trigonal and carbonium ion character is developed at C-4. As a result the proton on the Zn-co-ordinated alcohol is transferred to His-5 1. Hydride transfer from alkoxide to C-4 then permits the fast conversion of bent NADH to planar NADH.NPO p-nitrophenol octanoate I 7 t E EA $ EPO EQ E (NPO = p-nitrophenyloctanoate) Scheme 5 0 R-C-0 S- II R-C-OH 0 O \ v I1 R-'2-OH yRJn I H2O Scheme 6 " c.s. Tsai Arch. Biochem. Biophys. 1982 213 635. 392 C. A. Ross Alcohol dehydrogenase is known to have a broad substrate specificity catalysing the reversible oxidation of various primary and secondary alcohols. In addition it has other activities such as mediating the oxidation of aldehydes and hydrolysis of esters. It is this latter activity that has received further attention.34 Kinetic experi- ments were performed on the enzyme using p-nitrophenyl octanoate as substrate and the effect of chemical modification of arginyl sulphydryl and lysyl groups tested.The inhibition of the esterase activity by p-nitrophenol (non-competitively) and octanoic acid (competitively) support the Uni-Bi kinetic scheme shown in Scheme 5. The implication of cysteinyl and lysyl residues in the catalytic site is suggested by the results from chemical modification of these groups and thus Scheme 6 is proposed which resembles that of the sulphydryl esterases without however histidine activation of the cysteinyl group. Kinetic studies on two other oxido-reductases are worthy of mention here. It was recently rep~rted’~ that aldehyde reductase from pig kidney obeyed a strict compulsory-order mechanism coenzyme reacting first. On further e~amination,~~ the reverse reaction in the direction of alcohol oxidation exhibits random-order addition of substrates.Succinic-semialdehyde dehydrogenase from rat brain has also been re-investigated3’ and evidence produced for a compulsory-order mechan- ism coenzyme binding first though it was not possible to distinguish between a ternary complex mechanism and a Theorell-Chance mechanism. 6 Co-operativity Linking this section with the previous one is a report of pressure relaxation experiments3’ showing that the rate of NAD dissociation from liver alcohol dehy- drogenase is controlled by the rate of isomerization of the enzyme-NAD complex and that it is this isomerization which is the rate-determining step in the reduction of acetaldehyde. If this is the case it represents one of the first demonstrations of a rate-limiting conformational change in a dehydrogenase-catalysed reaction.Cornish-Bowden has published further observations on the mechanism of glucokinase from rat liver.39 Glucokinase is a monomeric enzyme with a single binding site for glucose on each molecule and yet which exhibits strong positive co-operativity. Thus the Monod and Koshland models do not apply and a kinetic model must be invoked. Rabin’s original idea of ‘enzyme memory’40 has been developed by Ricard et aL4’ into the so-called mnemonical mechanism. The model requires that the free enzyme exists in two forms with differing affinities for the substrate (glucose in this case) which give rise to the same complex. If the complex reacts fast enough at high ATP concentrations so that equilibrium between the free forms of the enzyme is prevented then apparent co-operativity of glucose binding is observed as the relative proportions of the two forms of the free enzyme change with increasing substrate concentration.At low ATP concentrations no Is W. S. Davidson and T. G. Flynn Biochem. J.,1979,177,595. I6 F. F. Morpeth and F. M. Dickinson Biochem. J. 1981 193,485. A. J. Rivett and K. F. Tipton Eur. J. Biochem. 1981,117 187. M. J. Hardman Biochem. J. 1981 195 773. I9 M. Gregoriou I. P. Trayer and A. Cornish-Bowden Biochemistry 1981,20 499. 40 B. R. Rabin Biochem. I. 1967,102,22C. 41 J. Ricard J.-C. Meunier and J. Buc Eur. J.Biochem. 1974 49 195. Biological Chemistry -Part (ii) Enzyme Chemistry 393 co-operativity will be observed since equilibration of free enzyme forms occurs.The model for glucokinase based on steady-state experiments follows an ordered binding sequence so that ATP does not bind to free enzyme. The isotope-exchange data now presented supports this model rather than one which includes random- order binding.42 In contrast to the previous example citrate synthase which catalyses the condensation of acetyl-CoA and oxaloacetate consists of two identical subunits each independently binding one molecule of acetyl CoA and oxaloacetate. The enzyme exhibits both ligase and hydrolase activity and it might well be thought that these two diverse reactions would occur at different sites. Preliminary evidence has now been to show that when the conformational change occurs in the enzyme in the presence of oxaloacetate the free enzyme representing the hydrolase is converted into a ligase.In the presence of both substrates the enzyme is reconverted to the hydrolase form upon the formation of the intermediate (3S)-citryl-CoA. Co-operativity is ruled out and it is suggested that on binding oxaloacetate a ‘hinged movement’ takes place unmasking catalytic groups and bringing the two binding sites into proximity (ligase form). Hexokinase is an important enzyme and is regarded as the pacemaker of glycolysis in brain tissue and in erythrocytes. It is subject to regulation by the product glucose 6-phosphate for the action of which two different mechanisms have been proposed. One mechanism has glucose 6-phosphate at an allosteric site remote from the active site whereas the other envisages glucose 6-phosphate acting as a simple competitive inhibitor by binding to the y-phosphate subsite of the ATP-binding region.An investigation of the reverse reaction44 shows that glucose 6-phosphate exhibits classical Michaelis-Menten kinetics with a dissociation constant in close agreement with the inhibition constant of glucose 6-phosphate in the forward reaction. From’m therefore maintains his earlier contention that regulation of hexokinase is a manifestation of product inhibition glucose 6-phosphate binding to a high-affinity site that is also the active site. Malate thiokinase catalyses the reversible formation of malyl-CoA or succinyl-CoA from ATP CoA and malate or succinate respec- tively.It is a tetramer each subunit being composed of two non-identical units. Incubation of the enzyme with succinyl-CoA leads to the formation of a tight complex in which four succinyl-CoA molecules are bound per tetramer.45 The ligand is released on denaturation of the enzyme by SDS or on the addition of ADP + inorganic phosphate. However addition of ATP results in the loss of two molecules of bound succinyl-CoA with concomitant incorporation of 2 molecules of phosphate into the enzyme. This enzyme form will combine with succinate plus CoA but will only release phosphate. Hence it is claimed for this enzyme that it displays half-of-the-sites activity. Finally in this Section is a report46 on that most investigated of allosteric enzymes aspartate transcarbamylase (ATCase).The kinetics of this enzyme are complicated by the fact that the holoenzyme is a dodecamer and contains separate 42 M. L. Cardenas E. Rabajille and H. Niemeyer Arch. Biol. Med. Exp. 1979 12 571 43 E. Bayer B. Bauer and H. Eggerer Eur. J. Biochem. 1981 120 155. 44 L. P. Solheim and H. J. Fromm Arch. Biochem. Biophyr. 1981 211 92. 45 L. B. Hersh and M. Peet J. Bid. Chem. 1981 256 1732. 46 J. Foote and W. N. Lipscomb J. Bid. Chem. 1981 256 11 428. 394 C. A. Ross catalytic and regulatory sub-units so that it does not easily conform to either the Monod or the Koshland models. The reverse reaction involving the formation of carbamyl phosphate and aspartate has now been studied using a new assay system involving the removal of products in order to overcome the unfavourable equili- brium position which strongly favours the forward reaction (Scheme 7).Under these conditions co-operativity is not observed. In connection with this novel assay system it may be noted that a method has appeared4' for optimizing the amount(s) of enzyme(s) used in coupling assays. carbamyl aspartate xpLse carbamyl phosphate aspartate a-ketoglutarate x transaminase xaloacetate dehydrogenase'"""XNAD+ malate glutamate Scheme 7 '' F. Garcia-Carmona F. Garcia-Cbnovas and J. A. Lozano Anal. Biochem. 1981,113 286.

ISSN:0069-3030    

DOI:10.1039/OC9817800381

出版商:RSC    

年代:1981

数据来源: RSC

摘要:

Author Index Aalstad B. 122 Abbott P. J. 12 Abdesaken F. 294 Abdul-Malik N. F. 235 Abe Y. 214 Abel E. W. 27 Abele W. 337 Abell C. 20 Abeywickrema R. S. 118 Abraham M. H. 65 Abramovitch R. A, 100 159 Acheson M. 35 Achiwa K. 355 Achmatowicz 0..jun. 59 Adam M. J. 216 Adam W. 143 Adams R. D. 62 196 Adcock J. L. 88 Adlington R. M. 179 239 Adolph H. G. 212 Adwidjaja G. 128 Afanas’ev I. B. 82 Agawa T. 251 262 266 Agirbas H. 82 215 Agosta W. C. 10 141 196 Ahlberg P. 70 201 Ahmed F. R. 234 Ahmed Z. 225 Aihara J. 44 Aime S. 19 28 Ainsworth S. 388 Akaba R. 201 Akgiin E. 221 Akhrem A. A, 60 Akiba M. 247 Akiyama T. 122 Aksnes G. 38 Akssira M. 176 AIAruri A.D. A, 212 Alberti A, 83 283 Albery J. W. 121 Albini A, 133 134 Alborz M. 78 Alder R. W. 201 Alexakis A, 148 156 307 Alexandratos S. D. 50 205 Alexandrov Yu. A, 81 Ali A. E. 367 Ah M. B. 52 Ali S. A, 184 308 31 1 Alibahi M. 76 Allinger N. L. 42 Almgren C. W. 201 Almlof J. 40 Alnajjar M. S. 295 Al-Omran F. 206 Alonso M. E. 113 Alper H. 160 234 255 Ames A, 335 Ames D. E. 269 Amin S. 228 Amino Y. 182 Amita F. 30 35 Ammann W. 15 Amos R. A, 175 Amrich M. J. 37 Anciaux A. J. 114 217 Andersen N. H. 326 369 Anderson B. 36 Anderson C. M. 388 Anderson D. R. 81 Anderson G. 60 Anderson G. H. 110 Anderson H. J. 243 Anderson M. W. 245 Ando W.115 218 234 Andrade J. G. 40 45 72 Andreou A. D. 210 211 Andrews L. 134 Angelastro R. 151 Angelini G. 68 Angliker H. 199 Angus R. 366 Anh N. T. 203 Anke L. 111 Ankner K. 128 234 Annunziata R. 184 Ansell M. F. 370 Anteunis M. J. O. 242 Antoni F. 36 Aoki S. 306 Aoyagi M. 227 Apeloig Y. 45 66 200 Apoussidis T. 87 294 Appel W. K. 229 Appleman E. H. 216 Applequist D. E. 89 395 Arad D. 66 200 Arai H. 250 Arai Y. 371 Arakawa K. 123 Archer W. J. 225 Ardecky R. J. 337 Aristoff P. A, 371 Ark D. 277 Armand J. 129 Armand M. 229 Armentrout P. B. 256 Armor J. N. 255 Armstrong D. R. 281 Arnold B. 113 Arnold D. R. 134 Arnone C. 212 Arrieta J.M. 190 353 Arthur G. D. 216 Arumi M. 205 Arvanaghi M. 286 Asai M. 236 Asano T. 29 30 33 Asao T. 269 Ashby E. C. 94 283 287 288 Ashe A. J. tert. 206 250 296 297 Asher V. 242 Askani R. 196 Askari S. H. 249 Atkinson R. S. 100 102 Atwood J. L. 293 Auchus R. J. 158 189 322 Audier M. 26 Austin W. B. 161 Au-Yeung B. W. 354 Avitabile G. 206 Avnir D. 87 Awad S. B. 235 Axen U. 373 Aydin R. 19 Ayyanger N. R. 252 Baan G. 363 Baba N. 170 Babiak K. A, 168 Bachmann P. 297 Back T. G. 152 396 Bacquet C. 121 Bkkvall J.-E. 267 276 Battig K. 194 244 334 339,344 Baggaley K. H. 367 Bagheri V. 112 Baici A, 385 Baillie P. G. 208 Baillie T.A. 3 Bainton H. P. 359 Baird M. S.,106 108 Baker R. 149 Bakuzis M. L. F. 114 Balci M. 199 Ballard J. M. 11 Ballester M. 213 Balli H. 105 Ballou C. E. 8 Bamkole T. O. 211 Ban Y. 124 Bandaranayake W. M.. 210 Bando M. 35 Banerjee A. K. 382 Bangar T. 135 Baraldi P. G. 363 371 Barber M. 10 11 Barcelos F. 366 Barco A, 363 371 Bardsley W. G. 385 Barendrecht E. 118 Baret P. 229 Barlet R. 112 Barlow J. J. 168 299 Barltrop 3. A, 144 Barluenga J. 151 152 251 284 289 Barnette W. E. 191 369 372 373 Baron R. P. 12 Barraclough P. 365 380 Barradas R. G. 119 Barrett A. G. M. 179 237 239 Bartlett P. A, 242 308 329 Bartlett R. J. 40 Bartmess J. E. 74 Barton D.H. R. 168 219 298 299 Barton T. J. 295 Bartroli J. 184 308 311 318 Bartsch R. A, 214 Baryshnikov Yu. N. 81 Basak A. 189 323 332 Basak S.,110 Batcho A. D. 57 Bates D. K. 206 Bates P. A, 208 Bates R. B. 44 Battye P. J. 23 77 Baudler M. 297 Baudouy R. 157 Bauer B. 393 Bauer H. 85 Bauer P. J. 78 Bauld N. L. 54 93 191 334 Baum K. 225 Baumann B. C. 5 Baumann R. 53 Bayer E. 393 Baysdon S. L. 166 Beak P. 45 Beats J. L. 351 Beauchamp J. L. 256 Beaulieu P. L. 160 163 Beck A, 64 Beck A. K. 316 Becker H. 225 Beckwith A. L. J. 185 Becu C. 242 Beddard C. 84 Bedenko V. 228 Beeckmans S. 387 Beeley N. R. A, 353 Begley M. J. 365 Begley W.J. 178 239 Begtrup M. 25 BCguC J.-P. 88 Behrens U.,60 Behringer H. 105 Bekhazi M. 106 Belanger D. 193 Beletskaya I. P. 283 Bell K. L. 327 Bellec C. 129 Belletire J. L. 55 191 Bellrille D. J. 54 93 191 334 Benard M. 40 Bender D. D. 153 269 Benetti S. 363 371 Benezra C. 175 Benner L. S. 210 274 Benner S. A, 21 59 194 Bennett S. G. 283 Bennett W. 149 Bennyarto F. 114 Bensadat A, 126 Benson S.W. 91 Benson W. R. 12 Bentley T. W. 66 Bentz P. 266 Berchtold G. A, 227 Berezin I. V. 222 Berg A. 225 Berg P. 381 Berger D. E. 57 Bergman R. G. 99 Bergsma J. P. 216 Bergstein W. 262 Bergstrom D. E. 271 Beringer F. M. 206 Berke C. M. 45 Berlin K. D.211 Bernad P. 151 Bernadou F. 161 Bernardi F. 40 Berry J. M. 216 Author Index Berski Z. 249 Berson J. A, 342 Bertholet J. 142 Bertran J. 205 Bertrand M. 57 345 Best W. M. 97 241 Beth L. D.. 213 Betts M. J. 179 Beyer M. 206 Beynon J. H. 5 7 Bhakta C. 366 Bhatt M. V. 221 Bianchi M. 255 Bidan G. 120 123 Biehl E. R. 221 Bierbaum V. M. 65 79 Biffar W. 18 Bigge C. T. 271 Bigot B. 46 47 Billingham N. C. 82 215 Bilow N. 161 Bindra J. S. 351 Bindra R. 351 Binger P. 266 Bingham R. C. 48 Bingmann H. 64 Binkley J. S. 39 Birch A. J. 320 Bird C. L. 130 Bird T. G. C. 193 Biro P. A, 383 Birtwell S. 214 Bitterman S. 36 Blackburn G. M. 228 Blackburn E.V. 93 Blacklock T. J. 112 Blake T. J. 8 Blakley C. R. 12 Blank N. E. 231 Blazejewski J. C. 298 Bloodworth A. J. 290 292 Blount J. R. 245 Bludssus W. 100 Blum J. 154 Blum W. 7 Blum Y. 275 Blurock E. S.,40 Bobbitt J. M. 122 Boche G. 202 Bock H. 99 Boden E. 339 Bodennec G. 126 Bodnar T. 256 257 Bockmann K. 229 230 231 Boekelheide V. 229 230 Bogdanovic B. 286 Boggs J. E. 40 42 Bohlmann F. 185 Bojesen G. 12 Boland W. 149 Bolster J. M. 245 Bolton R. 91 209 214 215 224 Bone W. M. 11 Author Index Bonfand A, 243 Bonfiglio J. N. 333 Bonini B. F. 283 Bonner D. P. 236 Bonnier J. M. 215 Booth M. 27 Borden W. T.,46,49,53,105 Bordoli R.S.. 10 11 Borg R. M. 134 Bos W. 189 Boschelli D. 189 Botteghi C. 255 Bottoni A. 40 Boudjouk P. 284 Boulton A. J. 246 Bourgeois J.-L. 261 Bourque R. A. 104 140 Bowen C. T. 66 Bowen R. D. 4 5 7 Bowers J. R. jun. 94 287 Bowmaker G. A, 209 Boyd D. R. 227 228 Boyer J. 75 Bradley C. V. 7 12 Bradsher C. K. 221 Brady W. T. 184 Brambilla R. 342 Branca S. J. 196 332 Branchini B. R. 68 Brand J. C. 85 Brandange S. 172 Brassard P. 337 Braunstein P. 258 Bray M. A, 351 Breeden D. L. 245 Brehm L. 248 Brennan J. 239 Brenton G. A, 5 7 Brereton R. G. 8 Breslow R. 54 Brettle R. 121 Brewster A. G. 219 Bridwell P. 169 Brinker U. H. 106 107 Brinkmeyer R.S. 165 Brisson C. 337 Brittain J. M. 209 Brockwell M. A, 365 Bronneke A, 181 Brook A. G. 294 Brooke D. N. 212 Brookhart M. 104 156 186 Brookhart T. 57 Brooks R. 172 Broom N. J. P. 219 Brothers P. J. 255 Broughton B. J. 362 Brousseau..~R..,~10 Brown C. D. 212 Brown H.C. 184 205 290 301 303 307 Brown R. F. C. 97 Brownbridge P. 176 Browne E. N. C. 334 Broxterman Q. P. 201 Broxton T. J. 76 Bruins A. P. 8 Brunelle D. J. 247 Brunner H. 282 Bryson T. A, 333 Brzezinski J. Z. 249 Bubnov Yu. N. 162 Buc J. 392 Buchanchenko A. L. 81 Buchi G. 340 Buck H. M. 85 Buckwalter B. L. 114 Budzikiewicz H.,3 6 Buechele J. L. 63 Buhler D. R. 228 Buhro W. E. 112 275 Bulbulian R.V. 210 211 Bull D. 269 Bumagin N. A, 283 Bumagina I. G. 283 Bunce N. J. 216 Bundy G. L. 351 370 379 Bunnett J. F. 66 71 Burgar M. I. 17 23 Burger U. 107 Burgess E. M. 50 Burk D. 381 Burke S.D. 193 Burkert U. 42 Burks S.R. 328 Burlingame A. L. 3 8 9 Burns T. P. 287 Burrell P. M. 16 Burrows C. J. 60 Bursill L. A, 26 Burton R. M. 213 Burton T. S.,362 Busch K. L. 11 Buschhaus H.-U., 87 294 Buse C. T. 184 314 315 Bush K. 236 Buske G. R. 206 Busker E. 6 Buss A. D. 149 304 Buter J. 182 Butler D. R. 127 Butler W. 234 297 Byers J. D. 367 Calado M. 36 Caldin E. F. 31 Caldwell A. G. 365 Caldwell C. G. 299 Caldwell G. 74 Callens R.242 Calvert D. 209 Cambell M. M. 237 Cameron D. 6 Cameron D. W. 60 223 Cameron T. S. 27 Camps P. 222 Canadell E. 205 Cane D. E. 67 Canonne P. 176 193 Canosa C. E. 82 Cantrell G. L. 322 Capizzi T. P. 384 Ciplar V. 184 255 Capon B. 75 Capon R. 225 Caramella P. 52 203 Carde R. N. 99 Cbrdenas. M. L.. 393 Cardillo G. 302 Carelli I. 130 Carini D. J. 189 323 Carlsen L. 182 248 Carmody J. J. 12 Carpenter B. K. 60 62 Carpita A, 306 Carrie R. 279 Carrion F. 48 Carriou M. 129 130 Carroll D. I. 8 Carroll G. L. 342 Carson J. R. 243 Carter M. J. 336 Caruso A. J. 328 Carver D. R. 180 213 Cassidy F. 367 Cassidy J. F. 23 77 Castaner J. 213 Castelhano A.L. 82 83 Caton M. P. L. 351 362 370 Catteau J. P. 83 Caulton K. G. 256 Causev. J. G.. 83 Cava k.P 225 337 Cave R. J. 190 357 Cavezzan J. 296 CerC V. 62 Chadwick D. J. 174 Chai R. 6 Chait B. T. 10 Chamberlin A. R. 303 Chan D. M. T. 194 265 324 Chan L. 114 Chan S. J. 384 Chan W.-T. 206 250 296 Chandrasekhar J. 40 41 43 44 45 72 203 285 Chang C.-A, 260 Chang M. J. 104 Chang S. 42 Chang Y. H. 100 296 Chao H.S.-I. 227 Chao-Jen Chung 81 87 Chapleo C. B. 356 Chapleur Y. 177 Chapman 0. L. 99 Chapuis C. 55 191 Charpiot B. 298 Chatgilialoglu C. 86 88 Chatterjee S. 281 Chatziiosifidis I. 325 Chautemps P. 229 Cheetham A. K. 26 178 Chen L.-C.249 Chen L.-J. 99 244 Chen T. Y. R. 217 Chen Y. S. 293 Chenard B. L.. 121 Cheng Y.-S. 55 340 Chiang S.-H. 139 Chiang W.-C. 387 Chidester C. G. 236 Chih-Yun Tu 339 Chini A, 292 Chinn J. W. jun, 286 Chitty A. W. 113 Chiu F.-T. 100 296 Chiusoli G. P. 269 Chizhov 0. S. 3 Cho H. 299 Choi H.-D. 59 Choi H. W. 273 Chollet A. 61 Chong A. K. A. 246 Chong J. M. 296 Chou C. S. 133 Chou S. S. P. 296 Chow Y. L. 84 Choy W. 184 310 Christensen S. B. 110 Christie R. M. 190 358 Christl M. 185 Christmas A. J. 362 Cieplak A. S. 203 284 Cimarusti C. M. 236 Cinquini M. 184 Claesson S.,38 Claramunt R. M. 25 Clardy J. 364 Claremon D. A, 243 379 Clark G.338 Clark H. R. 213 Clark T. 45 285 Clausen T. P. 70 Clegg W. 249 Cleland W. W. 388 390 Clementi E. 39 Clennan E.L. 201 Cliff C. J. 99 Cliffe I. A, 174 Cliffton M. D. 16 Clive D. L. J. 150 Clizbe L. A, 336 Cobbledick R. E. 208 Coceani F. 351 Coderre J. A, 17 Coe J. 389 Coffee E. C. J. 362 Cohen L. A. 247 Cohen S.G. 137 Cohen T. 322 323 Colcagno M.-P. 98 Coleman M. W. 214 Coleman R. A, 365 Collington E. W. 365 Collins S. 152 Collman J. P. 255 Colombo L. 171 Colonna F. P. 283 Colonna M. 209 Colonna S. 184 Colvin E. 316 Colwell A. R. 172 Coman G. 256 Comasseto J. V. 163 Comisso V. G. 184,255 Comita P. B. 99 Compton R. G. 121 Concell6n.J. M.. 151 Confalone P. N. 225 Conia J. M. 194 Conlin R. T. 43 115 294 Connolly J. W. 281 Consiglio G. 212 Constantin E. 8 Cook P. F. 388 390 Cook R. L. 42 Cooks R. G. 6 10 11 12 13 Cooley G. 174 Coombs M. M. 12 Coope N. J. 257 Cooper D. 183 Coppola G. M. 20 Corbet J.-P. 175 Cordova R. 58 Corell M. 225 Corey E. J. 299 335 376 378 Corfield G. C. 212 Cornish-Bowden A. 384 392 Corriu R. J. P. 75 Cortez C. 75 Costero. A. M.. 187 Cotter R. J. 8; 12 Court J. 215 Courtneidge J. L. 290 Cowley A. H. 293 Cowling A. P. 341 Craig T. A, 336 Cram D. J. 170 174 252 286 Crampton M. R. 212 Creary X.,71 Cremer D. 44 Crivello J. V. 219 Crljenak S.126 Cross P. E. 365 Crouse G. D. 62 64 192 354 Crow W. D. 108 Crowshaw K. 362 Cullen E.R. 307 Cullen W. R. 197 Curran D. P. 194 324 Curtis K. 50 Author Index Curtis M. D. 255 Cutler A. R. 256 257 Czochralska B. 130 Dahler P. 320 Dahlman O. 172 Dailly B. N. 91 215 Daley S.T. A. K. 244 Dalton J. C. 104 140 Damiano J. C. 284 Dammel R. 99 Damon R. 20 D’Angona J. 8 Danheiser R. L. 62 158 189 322 323 332 Danion D. 113 Danishefsky S.,335 336 Darcy P. J. 63 Darmanjan A. P. 38 Darst K. P. 302 Das B. C. 337 Das. P. K.. 89 Daub J. P. 177 Dauben W. G. 34 57 61 64 Davenport J. E. 91 Davidson E. R. 46 49 53 105 Davidson W. S. 392 Davies A.G. 87 92 201 Davies D. 238 Davies G. M. 252 Davies J. 190 357 Davies J. E. 168 Davies S. G. 282 Davis A. P. 248 Davis B. M. 128 Davis F. A, 235 Davis L. 41 337 Davis N. M. 243 Davis P. D. 104 140 245 Davis R. 359 Davoust S.G. 57 Dawson K. A, 228 Day A. C. 144 Day R. J. 10 11 D’Costa R. 234 De B. 369 Deacon G. B. 215 Debal A, 176 de Camp M. R. 221 De Chirico G. 148 304 Declercq J. P. 190 353 Dedeoglu E. 208 Defrees D. J. 39 40 45 Degani I. 169 Dehmlow E. V. 112 160 168 Dehnicke K. 196 Deiko S.A, 222 de Kanter F. J. J. 139 de la Mare P. B. D. 209 de Levie R. 224 Author Index Dell A. 8 12 Della E. W. 118 Demailly G. 177 De Mayo P.87 de Meijere A. 60 201 228 Demersman B. 259 Demonceau A. 114 217 Demou P. C. 17 Demuynck J. 40 Denis J. M. 63 236 Denney D. Z. 112 Depke G. 4 De Puy C. H. 65 79 Derouane E. G. 26 Derrick P. J. 3 Dervan P. B.,102 143 Deshayes C. 251 de Smet M.-J. 168 De Sousa Healy M. 241 Despax B.,83 Dessy F. 351 De Tar D. F. 42 Deutch J. 287 Deutsch E. A, 58 Devadas B. 98 Devaquet A. 47 DeVille G. 181 Dewar M. J. S. 41 48 de Wit P. P. 293 De Wolf B.,134 Dezube M. 303 Dhawan B.,232 Dhawan K. L. 221 Diakur J. 21 Diaz G. E. 93 Dickinson C. 24 Dickinson F. M. 392 Dickinson R. P. 365 Dielmann G. 8 Diephouse T. R. 297 Dieter R. K. 330 332 Dietrich H.285 Dike M. S. 193 Dill J. D. 44 Dillon K. B.,22 Dimsdale M. J. 357 DinCtiirk S. 82 215 Dinnocenzo J. P. 70 Dinya Z. 283 Di Rienzo B.,130 Disch R. L. 44 Ditto S. R. 245 Ditzel E. J. 208 Dixneuf P. H. 259 Dixon A. J. 362 Djuric S. 180 338 Dochwat D. M. 322 Dodsworth D. J. 98 Doecke C. W. 226 Dohrmann J. K. 88 Dolson M. G. 121 125 Domarev A. N. 117 Dombek B. D. 274 Donaldson R. E. 360 361 Donatelli B.A, 161 Doner L. W. 20 Doren K. 84 Dorow R. L. 112 275 Dotz K. H. 258 Dougherty R. C. 10 Douglas K. T. 78 Doyle M. P. 112 113 155 275 Drahnak T. J. 43 114 294 295 Drake A. F. 228 Draper M. 207 Dreiding A. S. 101 144 194 332 Drew G. M.18 Drickamer H. G. 31 Drouin J. 194 Druelinger M. 317 Dubac J. 296 Duckwall L. R. 172 Duddy N. W. 76 Diirner G. 139 Diirr H. 109 Duetsch H. R. 88 Dukes M. 353 Dunitz J. D. 198 Dunkin I. R. 108 Dupuis M. 39 48 Durham D. L. 16 Durst T. 221 237 Dusausoy Y. 258 Dussault P. 303 Dutly A, 208 Duus F. 182 Dynak J. N. 227 Eade R. H. A, 39 Easty D. M. 351 Easty G. C. 351 Eaton P. E. 196 Eberhardt M. K. 91 218 Eberson L. 95 125 213 217 Echter T. 63 Eckert-Maksif M. 23 Eckes H. 114 Eder V. 245 Edwards M. P. 340 Effenberger F. 76 221 Egert E. 176 Eggerer H. 393 Egsgaard H. 248 Ehrmann E. V. 98 Eilerman R. G. 192 325 Einhorn J. 121 Einstein F.W. B.,197 208 Eisenstein O. 203 Ejchart A, 16 Elbe W. 127 Elenien G. A, 118 Elguero J. 25 Eliel E. L. 171 Eling T. E. 367 Ellison R. H. 355 El-Mowafy A. M. 77 151 181,213 Elsevier C. J. 283 El-Shafie S. M. M. 213 El-Shiekh M. I. 221 Elving P. J. 130 El’yanov B.S.,30 Emokpae T. A, 212 Emoto S. 376 Emsley J. 24 Encinas M. V. 89 Enda J. 262 266 Endo M. 50 Endrenyi L. 384 Engdahl C. 70 201 Engelhardt G. 26 Engenito J. S. jun. 217 Ennis M. D. 318 Enokiya M. 271 Epiotis N. D. 72 Epstein J. 389 Epstein P. S. 255 Epsztajn J. 249 Erden I. 228 Erhardt J. M. 319 Erickson A. S. 181 Erickson G. W. 170 317 318 Eriksen J. 142 Ernest I. 252 Escudero J.187 Estreicher H. 335 Eto H. 123 Eumura S. 166 Evans D. A, 184 308 309 311 312 318 Evans D. R. 388 Eyring H. 4 Falmagne J.-B. 187 Fananas F. J. 284 Fanchiang Y.-T. 86 Farnell L. 205 Farnum D. G. 70 Farr W. 4 Farrant R. D. 174 Faure R. 19 Fauvarque J. F. 283 Fava A, 62 Fedorovich A. D. 60 Feher M. 297 Feldberg W. 351 Felkin H. 282 Feller D. 49 53 105 Fenske R. F. 47 Ferreira J. T. B.,163 Ferreira S. H. 351 Ferro M. P. 324 Feutrell G. A. 223 Feutrill G. I. 60 Fiandanese V. 148 304 400 Fiat D. 17 23 Fiaud J. C. 321 Ficini J. 194 Field F. H. 10 Field L.D. 206 Fields. K. W.. 320 Figeys' H. P.,' 234 Finch M. A. W. 190 355 356 374 Finn J.M. 167 Fisch J. 258 Fischbach U. 285 Fischer A, 208 Fischer H. 88 Fischer P. 104 186 Fischer W. 200 Fitzpatrick F. 370 Flammang R. 7 Flasch G. W. jun. 121 Flavell A. J. 228 Fleming I. 164 281 296 319,336,354 Flippin F. A. 291 Floor. T.. 165 Floyd D:M. 236 Floyd M. B. 351 Flynn T. G. 392 Fochi R. 169 Fogarasi G. 40 42 Fokkens R. H. 9 Folting F. 256 Foote C. S. 142 Foote J. 393 Ford T. M. 303 Forrester A. R. 84 Foscolos G. B. 193 Foster F. V. 224 Fourrey J.-L., 337 Fowler F. W. 55 243 340 Foxe M. A. 136 Franceschi G. 237 Francotte E. 244 339 Franken E. 222 Fraser-Reid B. 177 FrCchet J. M. J. 184 Frediani P. 255 Fredin L.197 Freerks R. L. 336 Freidlin G. N. 117 Freitag H.-A, 196 Frenna V. 212 Frey M. H. 25 Friary R. 342 Fried J H. 355 362 365 Friedrich L.E. 63 Friedrichsen W. 228 Friend E. W. 196 Frisque-Hesbain A. M. 190 353 Fritz H. 232 Frohlich R. 297 Fromm H. J. 393 Fruchier A, 25 Fry A. J. 118 128 234 Fuchs P. 118 Fuchs P. L. 360 361 Fueno T. 51 Fujimoto H. 50 Fujimoto K. 237 Fujisawa T. 271 Fujita H. 62 227 Fujita M. 249 Fujita T. 111 Fujiwara K. 206 Fujiwara T. 331 Fujiwara Y. 269 Fukata G. 219 Fukaya C. 335 Fukui K. 50 Fukumoto K. 236 Fukushima S. 56 Fukuzawa S. 158 Fukazawa Y. 227 Fukuzumi S. 79 210 289 Fuller S. E. 88 Fung A.P. 208 209 219 Furukawa N. 151 Furukawa Y.,182 Furuta N. 214 Fusaka T. 331 Fusco R. 222 Fushiya S. 174 Fuss A, 143 Fusser G. 113 Fyfe C. A, 26 Gadaginamath G. S. 228 Gadek T. R. 260 Gallagher T. 339 Galli C. 214 Galobardes M. R. 182 Galynker I. 184 198 Galzerano R. 50 Gambarotta S. 160 Gamble R. J. 142 Games D. E. 8 Ganapathy S. 26 Gandillon G. 107 Gandolfi C. 237 371 Gandour R. W. 61 133 Ganem B. 113 180 Ganguly A, 342 Ganis P. 206 Gano J. 99 Ganter C. 198 Garcia-CBnovas F. 394 Garcia-Carmona F. 394 Gardiner D. J. 32 Garratt D.G. 160 163 Garratt P. J. 226 Garret D. L.. 213 Garst M. E. 333 Garvey D. S. 184 308 311 Gasic G. P. 369 Gaspar P.P. 293 Gasparis-Ebeling T. 18 Gassner R. 242 Gasteiger J. 233 Author Index Gavina F. 187 Gdanski R. D. 89 Geisou H. P. 365 Gelin S. 251 Genet J. P. 194 277 Genies M. 120 123 Gennari C. 171 Geoghegan P. J. jun. 290 George M. V. 133 Georgiopapadakou N. H. 236 Georgoulis C. 159 Geret J. A, 17 Gerhard A, 232 Gerhardt W. 252 Germain G. 190 353 Gerson F. 202 230 Gesing E. R. F. 188 Gesson J.-P. 337 Gey C. 112 Ghaderi S. 8 Ghisalberti E. L. 225 Ghosez L. 187 190 353 Giacomelli G. 291 Giants T. W. 41 79 Gibbs H. W. 207 Gibson B. 212 Gibson K. H. 349 Gibson T. 154 Gierke W. 85 Giese B. 103 290 Giffney J. C. 206 Gil P. 187 Gilbert B. C.87 Gilbert W. 381 Gilchrist T. L.,226 242 250 Giles J. R. M. 84 85 Gill M. 190 358 359 Gilson J. P. 26 Giroldini W. 269 Gisler M. 222 Gladiali S. 255 Gladstone C. M. 55 Gleicher G. J. 89 Gleiter R. 285 Glinski M. B. 221 Glushkova A. A, 117 Goddard J. D.,39 43 47 49 Goddard W. A, 40 Godleski S. A, 66 200 263 Goel. A. B.. 283. 288 Gogan N. J, 243 Gold V. 23 Goldhill J. 319 Golding B. T. 169 Golding P. 212 Goldstein M. J. 70 Goldstein S.,190 353 Golembeski N. 196 Golitz P. 201 228 Golzke V. 87 Gopalan R. 75 Gordon D. J. 47 Gordon M. S. 43 115 Author Index Gordon R. L. 63 Gore J. 157 176 Gore P. H. 128 210 211 Gorman A. A, 51 Gorman R. 370 Gorrichon L.193 Goto T. 177 Gotor V. 251 Gourcy J. 120 Gower J. L. 8 Graeve R. 196 Grandbois E. R. 170 Gras J.-L. 340 Grasse P. B. 109 Grate J. H. 87 Grauer F. 212 Gray S. K. 110 Grayson J. I. 185 Grdina M. J. 141 Greathead R. J. 6 Greci L. 209 GrCe R. 279 Green G. R. 367 Greene R. M. E. 228 Greengrass C. W. 237 Gregoriou M. 392 Gregory R. B. 388 Grieco P. A, 243 364 Griesbaum K. 71 Griffin R. G. 25 Griffin T. S. 225 Grigg R. 276 Grigor’eva N. D. 295 Griller D. 37 82 84 89 92 109 Grimshaw J. 225 Grob C. A, 200 Grmland F. 36 Gross M. L. 8 Grotemeier G. 318 Grotjahn D. B. 326 Grudzinskas C. V. 351 Griiner H. 105 Grutzner J. B. 44 72 203 Gryglewski R. J. 350 Guanti G.76 171 Guelacar F. O. 120 Guenther H. 19 Guerra M. 83 283 Guidry R. M. 41 Guillemin J. C. 63 236 Gund P. 43 Gund T. M. 43 Gunther B. 200 Guo W. 112 Gupta D. N. 168 Gurak J. A, 286 Gurria G. M. 67 Gust S. L. 119 Gutekunst B. 294 Gutekunst G. 294 Guthrie R. D. 73 Gutsche C. D. 232 Guziec F. S. 307 401 Haberkorn R. A, 25 Hackenberger A, 109 Hacker N. 108 Hadicke E. 64 Hattori T. 290 Hauer J. 28 32 Hawari J. A.-A. 92 Hawkeshead E. 365 Hafelinger G. 206 Haenel M. W. 217 231 Hagen J. P. 184 Hagenbuch J.-P.,53 Hagiwara H. 189 Hakim H. G. 128 Hakushi T. 197 Hall L. D. 216 Hall S. E. 340 Halle L. F. 256 Halweg K. M. 191 Hamada Y. 115 Hayakawa K. 56 Hayashi M. 292 355 371 Hayashi T. 243 266 281 Hayasi Y. 266 306 359 Hayes J.C. 257 Hayes G. F. 212 Hayes P. C. 99 Hayes R. 250 Hays R. L. 74 Hazard. R.. 130 377 378 282 283 Hamaguchi H. 130 Hamamoto I. 92 Heathcock,’C. H. 175 184 308 313 314 315 Hamanaka N. 377 378 Hamann S. D. 30 38 Heather J. B. 359 Head M. A, 362 Hamberger H. 237 Hamel P. 243 Hecht S. M. 12 174 Hecht S. S. 228 Hamerlinck J. H. H. 85 Heck R. F. 153 269 Hamilton J. G. 228 Hamilton R. 61 Hamlet A. B. 237 Hedayatullah M. 101 Hegedus L. S. 255 Hehre W. J. 40 45 Hamper B. C. 167 Han B. 284 Heiberg A, 40 Heider J. 168 Hanack M. 68 Heimbach H. 6 Hanamura M. 43 115 Handa V. K. 128 234 Hanessian S. 177 376 Hanko R. 181 Hanreich R. 200 Heine H.-G. 186 187 Heinz K. J. 283 Helfer A. P. 293 Helgeson R. C. 174 Heller H. G. 63 Hansen P. E. 15 225 Hellmann J. 297 Harada T.109 182 Harakal M. E. 235 Hellwinkel D. 232 Helmchen G. 55 318 334 Harding K. E. 328 Hardman M. J. 392 Hardy C. J. 362 Hariu Y. 234 Helquist P. 104 156 186 Helsby P. 24 207 Henderson G. N. 208 Hendi S. B. 100 Harkema S. 63 Harpp D. N. 248 Harrer W. 85 Hendry D. G. 91 Henrici-Olive G. 210 Herbert D. J. 197 Harris C. J. 365 Harris J. A, 7 Harris R. L. N. 251 Heremans K. 30 Hermkens P. H. H. 85 Hernandez O. 376 Harrison A. G. 4 6 Harrison J. F. 103 Herold T. 184 Hersh L. B. 393 Hart D. J. 327 Hart H. 98 224 228 Hershberger J. 90 Hershenson F. M. 33.3 Hartman J. S. 26 Hertel L. W. 224 Hartmann W. 186 187 Hartshorn M. P. 208 Harvey K. 295 Harvey R. G. 75 224 2 Hasan I. 225 243 Hashihama M. 208 Hashimoto J. 155 Hassaneen H. M. 169 Hassner A, 234 Hata N. 81 Hata T. 237 Hatakeyama S.225 28 Herzig C. 233 Hess B. A. 44 Hess H. H. 118 Heuck K. 290 Heusler F. 216 Hevesi L. 71 Hexem J. G. 25 Heydt H. 114 Hidaka I. 208 Higgens R. 88 Higuchi H. 150 Hess U. 118 Higuchi K. 145 Higuchi T. 9 Hilgenfeld R. 252 Himizu J. 366 Hinz J. 186 Hioki T. 182 282 Hirai H. 111 237 Hirai Y. 236 Hiraki M. 275 Hirakubo K. 91 215 Hirama M. 184 311 Hirano S. 315 Hirao A, 170 Hirao T. 251 262 266 Hiraoka T. 237 Hirashima T. 163 Hirata F. 62 227 Hirokami S. 236 Hirota. F.. 39 Hirotsu K. 364 Hirst J. 211 212 Hishida S. 10 Hitchcock P. B. 252 Hiyama T. 261 315 Ho S. 227 Ho T.,-I. 136 Hodge P. 168 Hodgson H. H. 214 Hoesch L. 101 144 Hoff C. 281 Hoffmann D.228 Hoffmann R. W. 109 184 Hogeveen H. 70 201 Hogg J. L. 77 Hokawa M. 81 Holcomb W. D. 100 Holden K. M. 367 Holick W. 252 Holland D. 277 Hollander M. I. 307 Holmes J. L. 3 Holohan J. J. 353 Holton R. A, 269 360 Holwager W. 68 Holy N. L. 162 Honda S. 167 Hondo T. 236 Hong P. 272 Honohan T. 370 Hooper D. 103 Hoople D. W. T. 237 Hopkinson A. C. 43 Hoppe D. 181 Horak V. 224 Horgan A. G. 61 Horii T. 214 Horino H. 220 269 Horita K. 88 Hornby E. J. 365 Horner L. 99 Homing E.C. 8 Horsewood P. 59 Horton D. 192 Horton E.W. 350 Hosoe M. 385 Hosoya H. 39 Hosoya M. 278 Houge C. 190 353 Houk K. N. 45 51 52 56 61 83 103 112 133 203 285 334 Houlihan W.J. 97 Hout R. F. 40 Howard C. 357 Howard J. A, 89 Howard. S. I.. 170 Howbert J. J 56 Howe I. 7 Hoye T. R. 328 Hsiung H. M. 10 Hsu H. C. 152 Hsu-Lee L. F. 359 Hua D. H. 299 Hubbard C. D. 31 Hubbard J. L. 303 Hubbard J. S. 213 Huber W. 226 Hubert A. J. 114 217 Hudlicky T. 322 Hudson A. 283 Hudson C. E. 4 Hueber R. 8 Huffman J. C. 256 Hugueny J. C. 101 Humphrey M. B. 156 Humphrey P. T. A, 365 Hunkler D. 64 Hunt D. A. 221 Hunt D. F. 11 Hunt J. E. 10 Hunt P. G. 176 Hunter W. E. 293 Husk G. R. 104 186 Huskey W. P. 77 Hutchins M. G. K. 101 Hutton R. S. 108 Hwang J. 36 Hyla-Kryspin I. 40 Hylarides M. D. 152 Ibrahim I.T. 184 Ichikawa H. 205 Ichikawa Y. 177 Igeta H. 250 Iguchi M. 123 Iguchi S. 292 Iilima S. 259 Iimori T. 179 Iio H. 177 Ikariya T. 262 Ikeda H. 325 Ikeda M. 168 300 Ikeda N. 165 307 Ikegami S. 164 372 373 Ikeno M. 115 Ikota N. 113 Illingworth J. A, 387 Imada A. 236 Author Index Imagawa T. 122 Imanaka T. 275 Imashiro F. 206 Imperiali B. 184 310 Inagaki M. 101 Inagaki Y. 35 Inbar S. 137 Indge K. J. 385 Ing H. T. 208 Ingold C. F. 153 Ingold K. U. 84 86 88 89 92 Inoue H. 35 Inoue M. 249 Inoue N. 220 269 385 Inoue Y. 141 197 Inouye Y. 170 Inui. T.. 273 Ip D. P. 216 Ippolito R. M. 369 Ireland R. E.,177 Irie K. 124 Irikawa H.84 Isaacs N. S. 29 32 33 34 Iseki K. 372 Ishibashi H. 59 Ishida A, 366 Ishiguro M. 165 307 Ishihara Y. 177 Ishikawa H. 163 287 300 Ishikawa M. 115 281 292 Ishimoto S. 359 Ishino Y. 163 Ishizuka N. 355 Iskander G. M. 250 Ismail N. 118 Isobe K. 189 Isobe M. 177 359 Itagaki Y. 9 Itahara T. 269 Ito T. 135 Ito Y. 138 206 338 Itoh A, 291 Itsuno S. 170 Ives J. L. 51 Iwamura H. 17 143 Iwano Y. 237 Iwasa A, 208 Iwasawa N. 173 Iwata C. 331 Iwata S. 39 Iygengar R. 67 Iyoda M. 226 Izawa T. 179 Izawa Y. 114 135 Izumi T. 229 Jabri N. 148 156 307 Jackson A. H. 223 Jackson R. A, 82 90 215 Jackson R. W. 32 375 Jackson S. D. 275 Jackson W. P. 329 Jacobs S.A, 75 Author Index 403 Jadhav P. K. 184 301 Jaenicke L. 149 Jaffe H. 206 Jaime C. 222 Jakupovic J. 185 Jameson A. K. 16 Jameson C. J. 16 Jammar R. 234 Jancke H. 26 Janssen L. J. T. 118 Jansson. R. E. W.. 130 Jaquesy; J.-C. 337 Jardin J. 366 Jardine F. H. 255 Jarman M. 3 Jarosz S. 177 Jarvi E. T. 184 232 Jastrzebski J. T. B. H. 283 Jasys V. J. 237 Jautelat M. 277 Javaid K. 32 Jaw B. R. 286 Jawdosiuk M. 94 Jee J. 36 Jefferies P. R. 225 Jeffery-Luong T. 157 Jefford C. W. 51 Jelinski L. W. 68 Jeminet G. 120 Jemmis E. D.,43 285 Jencks W. P. 78 Jendrzejewski S. 247 Jenkins M. J. 205 Jenner G. 34 36 59 Jennings K. R. 6 Jennings L.J. A, 367 Jenny T. 19 Jerina D. M. 127 227 228 Jessup P. J. 336 Jimbnez C. 152 289 J~rgensen,F. S. 182 John L.-S. 63 Johnson G. 237 Johnson M. R. 177 Johnson R. A, 373 Johnson R. P. 47 Johnson W. D. 369 Johnston L. J. 87 Johnstone R. A. W. 148 Joly-Goudket M. 282 Jones D. J. 24 Jones G. 99 139 Jones J. W. 224 Jones M. jun. 104 Jones R. A. 293 Jones R. C. F. 245 Jones W. M. 97 199 Jonsall G. 70 201 Jonsson L. 95 213 Jorgensen W. L. 44 72 203 Josefiak C. 30 Jouin P. 170 252 Jbiwiak A, 249 Jubault M. 130 Judkins B. D. 100 Julia L. 213 Julien J. 234 Jung M. E. 55 191 337 Juri P. N. 214 Juriew J. 137 231 Jutand A. 283 Kabalka G. W. 152 169 180 Kadonaga J.T. 158 189 322 Kagotani M. 159 182 Kahle A. D. 20 Kahn L. R. 39 Kaim W. 283 284 Kaiser E. T. 78 Kaji A. 92 Kajihara Y. 153 259 260 Kakushima M. 243 Kale V. N. 150 Kalinowski H.-O. 196 Kallury R. K. 294 Kaloshina. N. N.. 81 Kambara,'H. 10 Kambe N. 139 Kametani T. 53 185 236 329 337 380 Kamiyama S. 229 Kamlet M. J. 24 Kamounah F. S. 210 Kanarek L. 387 Kane M. P. 236 Kaneda K. 275 Kanehira K. 282 Kanematsu K. 56 Kang H. C. 229 Kanuma N. 174 Kao J. 205 Kao L.-C. 153 269 Kaptein R. 139 Karni M. 4 Karpf M. 194 332 Karpov G. V. 9 Karras M. 58 Kasahara A, 229 Kashin A. N. 283 Kashiwagi H. 39 Katakuse I. 9 Kataoka H.265 Katayama S. 125 292 Kates M. R. 69 Kato M. G. 385 Kato S. 42 49 Katritzky A. R. 77 151 181 213 249 Katsuki T. 168 300 Katz J. J. 10 Katzenellenbogen J. A, 175 216 319 Kaufmann E. 44 72 203 Kaur H. 90 Kawabata N. 155 Kawada Y.,17 Kawakami Y. 157 Kawamura A. 241 Kawamura M. 371 Kawamura S. 214 Kawanisi M. 122 Kawasaki T. 9 Kawauchi H. 278 Kayzad A. 250 Kazarinoff M. N. 387 Kebarle P. 5 Keck G. E. 59 339 345 Keeffe J. R. 78 Keelan B. W. 134 Kees F. 235 Kelleghan W. J. 161 Kellogg R. M. 170 182 245 252 300 Kelly A. G. 375 Kelly D. P. 205 Kelly D. R. 357 Kelly L. F. 320 Kelly M. G. 191 Kelly R. C. 375 Kelm H. 29 30 Kemper B.184 Kenan W. R. jun. 171 Kende A. S. 225 Kenley R. A, 91 Kennard O. 176 Kennedy I. 350 365 Kenyon G. L. 388 Kerber R. C. 104 156 186 Kerdesky F. A. J. 184 310 337 Kerr I. S. 121 Kessel C. R. 34 Kester T. C. 287 Keumi T. 219 Kevill D. N. 65 66 Khan M. A, 121 Khatri N. A, 339 Khudyakov I. V. 38 Kielbasinski P. 184 Kikuchi J. 232 Kikuchi O. 61 133 Kikukawa K. 220 Kilbourn M. R. 216 Kilnger F. 224 Kim J. A, 260 Kim J.-I. I. 153 269 Kim J. R. 36 Kimura K. 62 227 261 315 Kimura M. 140 King B. A, 287 King H. F. 39 King K. D. 87 Kingsbury C. A. 16 Kira M. 84 Kirby G. W. 59 Kirchen R. P. 69 201 Kirk D. N. 174 Kirk T. C. 58 Kirmse R. 121 404 Kirmse W.109 140 199 Kise N. 151 Kishi Y. 177 225 308 Kistenbriigger L. 128 Kita H. 129 Kita Y. 249 Kitano K. 236 Kitaura K. 40 48 Kitchen J. P. 298 Kitching W. 18 295 Klhrner F.-G. 60 186 Kleemann A, 262 Kleijn H. 283 Kleimann W. 246 Klein J. 112 Klein R. D. 383 Klein T. P. 264 Klerks J. M. 283 Kleschick W. A, 175 314 Klimke G. 32 Klingebiel U.,249 Klinowski J. 26 Kloosterziel H. 202 Klumpp G. W. 111 284 Klunder A. J. H. 189 Knapp S. 335 Knifton J. F. 274 Knipe A. C. 211 Knolle J. 376 Know G. R. 307 Kobayashi K. 17 Kobayashi M. 214 225 359 Kobayashi S. 179 Kobayashi T. 272 Kobayashi Y. 189 265 Koch T. H. 144 Kochi J.K. 79 210 214 289 Koehler K. F. 178 239 Konig L. 107 Koppel B. 101 Koester K. 130 Koster R. 252 Koga N. 50 Kohn M. 212 Kohno S. 262 Kok D. M. 201 Kollmar H. 48 Komatsu M. 145 Komin A. P. 213 Komiyama M. 11 1 Komori T. 9 Kondo K. 139 Kondo M. 114 Konieczny S. 293 Konishi M. 266 281 Konishi Y. 355 371 Kono K. 220 Koob R. D. 43 115 Koppes W. M. 212 Kornblum N. 181 Korth H.-G. 83 Kos A. J. 285 Kossai R. 128 Koster N. H. 236 Kosuge S. 378 Kosugi H. 189 Koszyk F. J. 322 Kotsuki H. 241 Kouba J. K. 195 Kowalski C. J. 320 Koyama K. 99 Koyanagi M. 272 Kozikowski A. P. 244 335 Kraeutler B. 81 133 Kralj B. 5 Kratzer H. J. 156 Kraus G.A, 244 344 Kraus K. K. 246 Krause L. J. 110 288 Krautwurst K.-D. 222 Krebs A, 199 202 222 Kreher R. 252 Kreiling G. 196 Kremer K. A. M. 104 156 186 Kresge A. J. 73 79 Kress A. O. 100 Kreutter N. M. 91 Krishnan R. 39 Kriste B. 85 Krogh-Jespersen K. 44 103 Krohn H. 88 Kronenbitter J. 19 Kropp P. J. 133 155 186 Krosgaard-Larsen P. 248 Kruizinga W. H. 300 Krunbholz E. 242 Kubo K. 19 227 Kubota E. 9 Kiindig E. P. 287 Kuhn A. T. 130 Kuivila H. G. 295 Kukolija S. 239 Kulkarni C. L. 122 Kulkarni P. S. 8 Kumada M. 115 243 266 281 282 283 292 Kumagai T. 246 Kumagai Y. 278 Kumar P. 247 Kunihiro F. 9 Kunz G. 127 246 247 Kuokkanen T. 36 Kurek J. T.290 Kurobe H. 329 Kuroda T. 197 Kurosawa H. 290 Kurozumi S. 359 Kurreck H. 85 Kurskii Yu. A, 81 Kurth M. 55 191 334 Kurth M. J. 328 Kurz M. E. 217 Kusano Y. 33 Kutzer J. C. 144 Kuzmin V. A. 38 Kwang Yul Choo 91 Author Index Kwantes P. M. 11 1 Kwart H. 61 Kwart L. D. 61 Kwok S. C. M. 384 Kwun 0.C. 36 Kyba E. P. 296 Laali K.. 23 Lablache-Combier A, 63 83 236 La Croce S. 256 Ladika M. 110 Lage H. W. 188 Lagow R. J. 286 Laeuzza. B. C.. 180 Laiti P.' M.,162 Lai Y.-H. 210 274 281 Laidig W. D. 44 Laidler D. A, 277 Lakshmikantham M. V. 337 Lallemand J. Y. 176 Lam P. Y.-S. 63 Lambert C. 256 Lambert J. B. 16 Lampe J. 184 313 314 Lang S. A,,jun.249 Lantzsch R. 271 Lapham D. J. 292 Lapin S. 217 Laporterie A. 296 Lappicirella A, 41 Larcheveque M. 176 Lardicci L. 291 Larock R. C. 282 Larson J. R. 72 Lashley L. K. 283 Lattes A, 83 Lau K. S. Y. 161 Laurent E. 126 Laurian L. G. 236 Lavalle P. 376 La Voie E. 228 Lawrance G. A. 29 Lawrence G. W. 212 Lawson J. P. 180 Le A. T. 67 Leach D. R. 282 Ledford E. B. jun. 8 Ledwith A, 144 Lee H. 228 Lee K. 260 Lee K. H. 91 215 Lee M.-G. 387 Lee P. E. 301 Lee S. H. 296 Lee S. S. 359 Lee T. V. 319 356 357 Lee. W.-B.. 103 Lefort D. '88 Leger S. 177 Le Goaller R. 112 Le Goff E. 241 Legueut Ch. 176 Author Index Le Guillanton G.125 Lehnig M. 84 Lehr F. 316 Lelandais D. 121 Le Mahieu R. A. 220 Lemay G. 176 193 Lemieux R. U.,153 Le Moing M. A, 125 LCna. L.. 19 le Noble; W. J. 29 30 36 38 110 Leonard N. J. 27 Lesko P. 355 Lessard J. 84 Lester D. J. 298 Lester W. A. 48 Letendre L. J. 319 Leuenberger C. 101 144 Leung K. H. W. 90 Leuschner R. 88 Levi B. A. 45 Levin M. D. 12 Levine S. G. 192 Levsen K. 6 Levy A. B. 151 243 Levy G. P. 365 Lewis E. 8 Lewis E. S.,205 Lewis F. D. 63 136 Lex J. 226 Lev. S. V.. 219. 329. 340 Leiendecker F. 194 Li P. T. J. 287 Li T. T. 355 Libs S. 36 Lichtenberg F. 181 Liebeskind L. S. 166 Liebman J. F. 103 Liehr J. G. 7 Lien M. H.43 Lifshitz C. 4 Light L. 337 Liliefors T. 231 Lin L. C. 243 Lin Y.-I. 249 Lincoln F. H. 351 373 Linderman R. L. 324 Lindsay D. A, 92 Lindsay Smith J. R. 88 Lineweaver H. 381 Linfield W. M. 172 Lingenfelter D. S.,174 Linscheid M. 8 Linschitz H. 137 Linstrumelle G. 157 Liotta C. L. 50 Lippmaa E. 26 Lipscomb W. N. 388 393 Lis R. 335 Lissel M. 160 Lister S. G. 340 Little R. D. 342 Liu H.-J. 334 Liu K.-C. 138 Liu K.-T. 205 McGuire J. 370 Liu L. K. 11 Machado-Araujo F. W. 176 Liu W. C. 236 Machinami T. 192 Livingston D. C. 12 Mack A. G. 144 Lloyd R. V. 83 McKellar B. C. J. 209 Loader C. E. 243 McKelvey R. D. 17 Lockhart T. P. 99 McLafferty F. W. 3 5 12 Lodge E.A, 26 McLaren S. L. 21 Logemann E. 232 MacLeod J. K. 5 Logusch E. 177 McLuckey S. A, 6 Lohmann J.-J. 250 McManus S. P. 159 172 Lombardi P. 237 McNab H. 108 244 Lombardo L. 330 McNamara J. M. 225 Longo A. 237 McNeal C. J. 10 Longuet-Higgins H. 228 McPhail A. T. 234 342 Looker J. H. 16 Maeda H. 59 Loosen K. 109 199 Magi M. 26 Lopez J. 202 230 Maetani I. 9 L6pez-Ortiz J. F. 251 Maggio J. E. 21 194 195 Lory E. R. 12 Maggiulli C. A. 229 Lott K. A. K. 128 Magnus P. 180 338 339 Lotze M. 109 Magolda R. L. 191 340 Loupy A. 74 372 373,379 Lowe G. 178 239 Mah T. 23 Lowe J. P. 228 Maier G. 188 189 196 294 Lozano J. A, 394 Maier W. F. 42 196 Luche J. L. 284 Maifeld W. 60 186 Liibbert A. 86 Maillard B. 92 Liidemann H.-D.28 32 Main L. 207 Liinig U.,290 Maitlis P. M. 255 Luis S. V. 187 Maitte P. 129 Lukacs G. 15 Makagawa T. 226 Lumley P. 365 Malatesta V. 89 Lund H. 118 129 Malek F. 90 Lupo A. J. jun. 55 340 Mahotra R. 206 Lusztyk J. 87 201 Malik K. V. 351 Lynch J. E. 171 Mallamo J. P. 173 Malleron J.-L. 321 Mallion K. B. 353 Ma E. C. L. 293 Malloy T. B. 42 Ma P. 184 310 Malone J. F. 228 Maas G. 99 Malpass J. R. 102 McAdoo D. J. 4 Malrieu J.-P. 43 McCabe P. J. 365 Malsch K.-D. 188 196 McCabe R. W. 252 Mal’tsev V. I. 81 McCague R. 226 Manabe O. 33 136 252 McCarry B. E. 248 Mandal A. K. 184 301 Maccioni A, 283 Mandelbaum A, 4 McClelland R. A, 76 Mander L. N. 330 McCloskey J. A, 7 Manglik A. K. 208 McCollum G.W. 180 Mann J. 341 McDaniel R. L. 192 Manning T. D. R. 133 MacDonald J. G. 247 Manring L. E. 142 McDonald R. 243 Mantei N. 384 McDonald R. C. 388 Mantello R. A, 205 Macdonald T. L. 91 165 Man-Wing Tse 92 317 Manzo R. H. 213 McDowell C. A, 26 197 Mao C. R. 63 McFadden W. H. 3 Maquestiau A, 7 MacFarlane R. D. 10 Marazano C. 337 McGee L. R. 184 312 31 8 Marazza F. 194 McGilvery D. C. 5 March G. 82 215 McGuilay P. B. 385 March J. 217 McGuinness S. J. 211 Marchese G. 148 304 406 Mareda J. 107 Margaretta P. 120 Mariani H. A, 127 228 Marinelli E. R. 151 243 Marino J. P. 191 324 Marks A, 221 Maroldo S. G. 206 Marosfalvi J. 363 Marquet J. 264 Marquez J. 117 Marriott P. R. 37 82 89 Marsella J.A. 256 Marshall P. D. R. 87 Marshall R. M. 82 Marsmann H. C. 18 Marteau P. 30 Martelli J. 279 Martens J. 262 Martigny P. 120 Martin S. F. 339 Martin V. S. 168 300 Martinez G. R. 243 Martinez-Davila C. 62 158 189 322 Maruoka K. 292 333 Maruyama K. 177 184 313 315 Maruyama O. 269 Maruyama Y. 9 Marziano N. C. 205 Masaki C. 166 Masaki H. 32 Masamune I. 184 Masamune S. 184 308 310 311 Masamune T. 239 Maschmeier C. P. 129 Mash E.. A, 67 Mashima K. 153 259 260 Maskill H. 196 Mason J. 16 Mason S. F. 228 Mataka S. 244 Mateoli U. 255 Mathre D. J. 318 Math S. A, 114 Matossian V. 389 Matschiner M. 129 Matsubura S. 359 Matsuda H. 9 273 Matsuda T.220 Matsumoto A. 127 Matsumoto H. 295 Matsumoto K. 35 Matsumura Y. 122 124 125 241 Matsuo T. 9 Matsushita H. 270 281 306 Matsuura T. 51 138 206 Matt D. 258 Matta K. L. 168 299 Matteson D. S. 307 Matturro M. 62 196 Matusch R. 188 Matz J. R. 322 323 Maul R. 105 Maxey K. M. 351 379 May D. D. 86 Mayer W. 196 Mayr H. 44 72 203 Mazaleyrat J.-P. 170 286 Mazenod F. P. 143 Mazerolles P. 296 Mazza D. D. 244 Mazzanti G.. 283 Mehdi S. 17 Mehrotra M. M.. 365 Meier H. 63 137 231 Meijer J. 283 Meinetsberger E. 105 Meinhart J. A, 263 Melan M. 232 Menard K. 256 Mende U. 196 Menzel D. B. 367 Merbach A. E. 30 36 Merkuschew J. 137 231 Mersh J.D. 197 Mertes M. P. 271 Mesnard D. 161 Meth-Cohn O. 99 250 Meul T. 226 Meunier J.-C. 392 Mews R. 100 Mever. F. K.. 36 Meiers A. I 170 173 180 311 317 318 Micheau J. C. 83 Michl J. 43 114 294 295 Michna P. 335 Michno D. M. 64 Midland M. M. 301 Miginiac L. 161 M’Halla F. 117 Mihelich E. D. 142 Mihm G. 294 Mikhailov B. M. 162 Mikolajczyk M. 184 Miles W. H. 61 Miller A. L. 213 Miller D. J. 263 Miller J. 212 Miller J. A, 149 304 Miller J. M. 24 Miller V. R. 17 Miller W. H. 110 Milner D. J. 276 277 Minabe M. 225 Minami I. 325 Minato A, 243 283 Ming-Fea Chow 81 87 Minoun H. 153 Miri A. Y. 210 Mironev V. A,,60 Mischler D. 258 Mise T. 272 Mishina T.208 Mishra S. P. 218 Author Index Misic-Vukovic M. 213 Mislow K. 42 Mispreuve H. 7 Misumi S. 150 Mitchell D. J. 46 Mitchell P. A, 5 1 Mitchell T. N. 18 Mitchell T. R. B. 61 276 Mitra A. 133 351 Mitra D. K. 365 Mitsudo T. 279 Miura K. 168 173 Miura S. 359 Miwa G. T. 384 Miwa H. 276 Miyake H. 92 Miyake T. 300 Miyamoto T. 130 Miyamura S. 355 Miyaura N. 156 223 306 Miyoshi H. 158 Mizakami M. 130 Mizobuchi S. 363 Mizutani M. 182 Mo S. H. 293 Mochida K. 84 Mochizuki T. 236 Mock G. B. 104 Modrich P. 383 Morch L. 172 Moffatt F. 55 191 334 Mohnhaupt M. 55 191 Molander G. A, 307 321 Molas J. 222 Moncada S. 350 Mondon M. 337 Montgomery S.H. 184 313 Montpert A, 279 Moodie. R. B. 23,77,207,208 Moody C. J. 226 245 Moore M. W. 148 270 291 3 04 Moore R. N. 21 Moore R. W. 367 Moore W. B. 66 200 Moracci F. M. 130 Moran P. J. S. 212 Morel J.-P. 31 Morel-Desrosiers N. 31 Moreno-Mafias M. 264 267 More O’Ferrall R. A, 205 Morgans D. J. jun. 177 Morge R. A, 375 Mori I. 61 Mori. S.. 184. 311 Moriarty R. M. 63 Morild E. 29 38 Morin J. M. 189 322 332 Morishita T. 151 Morisset V. M. 160 163 Morita S. 56 Morley J. 351 Morokuma K. 39 40 42 43 48 49 115 Author Index Morosawa S. 140 Morpeth F. F. 392 Morris D. F. C. 211 Morris H. R. 3 11 12 Morris J. 336 Morris K. P. 23 Morrison J.A, 110 286 288 Morrison J. D. 170 206 Morrison J. J. 184 308 314 Morten D. H. 66 Morton H. E. 296 Morton J. A. 329 Mory Y. 384 Mosbach K. 387 Moss R. A, 103 104 107 112 Moss S. F. 249 Motherwell W. B. 168 298 299 Motokawa K. 239 Mudryk B. 94 Miillen K. 226 Mueller P. H. 103 Miiller S. 222 Miiller W. M. 252 Muetterties E. L. 273 275 Muggleton B. 92 Mujata S. 338 Mukai T. 53 Mukaiyama T. 170 173 179 Mukerjie A. K. 247 Muller G. W. 342 Muller L. 185 Murahashi %-I. 147 Murai A, 239 Murai S.,139 Murakami K. 239 Murakami M. 158 Murase M. 122 Murata I. 227 252 Murata S. 167 Muroi M. 236 Murphy C. J. 307 Murphy W. S. 66 219 Murray E.B. 172 Murtiashaw C. W. 193 Muscio 0.I. jun. 213 Mustafa A, 138 Musumarra G. 213 Muthukrishnan R. 232 Muzart J. 61 Myers A. G. 340 Myhre P. C. 26 71 Nader R. 228 Nagai T. 101 Nagai Y.,295 Nagaoka N. 177 308 Nagarajan N. 365 Nagase S. 43 115 Nagashima T. 325 Nagasura K. 153 259 260 Nagata M. 236 Nagata S. 384 Nagira K. 220 Nagy J. B. 26 Nagy J. O. 344 Nahm S. 286 Naito A, 26 197 Nbjera C. 152 289 Nakabayashi T. 214 Nakadaira Y. 295 Nakagawa K. 115 Nakagawa K. I. 292 Nakagawa M. 226 Nakahama S. 170 Nakai H. 292 Nakai T. 127 Nakaji T. 136 252 Nakajima H. 129 Nakakishi H. 16 Nakamura A, 153 259 260 Nakamura K. 206 Nakanishi S. 242 Nakao S.163 Nakashima T. T. 21 Nakashita Y. 125 Nakasuji K. 252 Nakata T. 303 Nakatani Y. 8 Nakatsuka M. 338 Nakatsuyama S. 174 Nakayama A, 236 Nakaya T. 3 1 Nakazaki M. 232 Nakazawa T. 227 Nakazumi H. 214 Nambiar K. P. 177 Nanninga T. N.,47 Naoshima Y. 363 Nara M. 359 Narang S. A, 10 Narang S. C. 208 209 Narayanan B. A, 317 Narine B. 250 Narisano E. 171 Narita N. 218 Narula A. S. 320 Naruse K. 271 Nasehzadeh A, 65 Naser-ud-Din 112 Nashed N. T. 78 Naso F. 148 304 Nassr M. A. M. 290 Natalie K. J. 269 Nathans D. 383 Natori Y. 262 Neckers D. C. 245 Neef G. 245 Neff J. R. 66 200 Negishi E.-I. 148 162 270 281 290 291 304 306 Neill J. D. 228 Nelsen S.F. 201 Nelson G. O. 156 Nelson J. V. 184 308 309 Nelson N. A, 375 Nemoto H. 53 185 329 337 Neszmelyi A, 15 Neuenschwander K. 244 Neuman R. C. 37 Neumann W. P. 87 293 294 Newcombe P. J. 100 Newman P. 209 Newsam J. M. 178 239 Newsom J. G. 99 244 Newton R. F. 174 190 191 347 355 356 357 362 369 374 Newton T.W. 164 296 Ney P. 149 Ng J. S. 216 Ngoviwatchai P. 217 Nguyen T. T. 87 Niazi S. 24 Nibbering N. M. M. 9 65 Nicolaou K. C. 191 243 328 331 340 369 372 373,379 Nicolas. E. C.. 73 Nicovich J. M.,91 Nidy E. G,, 373 Niemeyer H. 393 Nilsson K. 387 Nisbet M. P. 22 Nishi S. 182 Nishida A, 164 Nishida I. 313 Nishida K. 62 227 Nishida S.158 Nishida T. 73 Nishiguchi I. 163 Nishimura Y. 42 Nishio K. 128 Nishitani K. 149 Nishiyama A, 123 Nishizawa M. 170 No K. H. 232 Nobbs M. S. 237 Noels A. F. 114 217 Noth H. 18 Noguchi Y. 138 Nohara T. 9 Nomoto K. 174 Nonaka T. 118 Nordberg R. E. 267 Nordlander J. E. 66 200 Norman R. 0. C. 87 88 Normant J. F. 148 156 307 Norris R. K. 94 100 North P. C. 370 Noto R. 212 Novack V. J. 297 Novak L. 351 359 363 Nowlin J. G. 8 Noyori R. 73 167 170 278 313 Nozaki H. 61 261 270 276 291 315 Nozoe S. 174 408 Author Index Nudelman N. S. 212 Nunes V. 36 Olli L. K. 196 Ollmann G. W. 127 Palfreyman M. N. 362 Palleros D. 212 Nunomoto S. 157 Nwaedozie J.M. 212 Nwokogu G. 228 Nystrom J. E. 276 Olsen E. G. 64 Olsson T. 231 O’Mahony B. 66 O’Malley R. F. 127 228 Onan K. D. 342 Pallini L. 269 Palmer T. 381 Pang F. 40 Pang P. P. 27 Panico M. 11 Ong C. W. 260 Pannan L. J. H. 223 Oae S. 151 218 Onishi T. 303 Paolucci C. 62 Obana M. 262 Obara S. 39 40 48 Oberrauch E. 125 217 O’Brien D. H. 245 Ochi M. 241 Ono N. 92 Ono R. K. 336 Onszowy H. 295 Onuki Y. 42 Onyido I. 211 Papadopoulos M. 34 59 Papahatjis D. P. 243 Papoula M. T. B. 298 Paquette L. A, 62 64 70 192 194 224 239 335 Oda J. 170 Oda M. 168 299 Odaira Y. 62 221 Opella S. J. 25 Oppenheimer L. 384 Oppolzer W. 55 57 185 354 Paradisi C. 66 Pardini V. L. 118 Oddershede J. 105 191 193 194 244 334 Parker T. 362 O’Dell D. E. 91 317 339,344 Parker V. D. 120 122 bzaslan N.90 Oppusunggu D. 16 Parker W. L. 236 Offen H. W. 30 Or Y. S. 196 Parlar H. 53 Offenbach J. L. 197 Orchin M. 255 Parmar S. S. 249 Oeata. M.. 205 Orena M. 302 Parrino V. A. 97 Ogata; Y.,’218 Ogawa T. 136 252 Ogle C. A, 44 Ogumi Z. 128 Ogura F. 150 Ogwa K. 359 Ohara E. 150 Orfanopoulos M. 58 141 Orgee L. 228 Orihara Y. 74 Orrell K. G. 27 Ortiz M. 159 Ortlieb H. 232 Osa T. 141 Parry M. J. 365 Parsons I. W. 216 Parton B. 242 Pastra-Landis S. C. 388 Pate B. D. 216 Patel B. A. 153 269 Patel K. B. 87 Ohashi M. 12 Osakada K. 262 Patel R. C. 181 Ohfune Y. 174 Osamura Y. 39 48 110 Paterson I. 319 Ohgi T. 174 Ohgo Y. 262 Ohmizu H. 151 Osawa E. 42 56 Osella D. 19 28 Oshima K. 61 270 291 Paterson P. E. 165 Paton J. 357 Patterson. J. W.. 362 Ohnishi H. 250 Ohno M. 179 Oshiro Y.251 Osugi J. 30 31 35 Paudler W. W.,’147 Paul W. 351 Ohrui H. 376 Otsubo T. 150 Pearlman B. A. 225 Ohsawa A, 250 Ohshiro Y. 262 266 Ohta T. 74 Otsuji Y. 242 Otsuka T. 295 Ott K. H. 9 Pearson A. J. 260 Pearson G. D. N. 257 Pearson M. J. 238 Ohuchida S. 377 378 Okada H. 290 Otto M. 121 Ourisson G. 8 Pearson N. R. 300 Pechine J. M. 234 Okada S. S. 168 Okado T. 33 Overill R. E. 24 Overman L. E. 291 327 Pederson C. Th. 105 Pedulli G. F. 83 283 Okamato Y. 34 167 20 5 335 336 Peel R. 353 Okamoto H. 232 Owada H. 150 Peet M. 393 Okamoto I. 167 Okamoto T. 74 Owen R. C. 136 Owens W. 364 Pellegrin V. 25 Pelter A, 174 Okamura N. 9 Ozawa S. 291 Pelus L. M. 351 Okano M. 150 158 Pennings M. L. M. 63 Okawara M. 306 Okazawa N. 69 O’Krongly D. 55 191 Oku A, 109 Okude Y.315 Pac C. 135 217 Pacansky J. 83 Paddon-Row M. N. 52,61 83 133 203 Percival A. 336 Perera C. P. 234 Pereyre M. 281 Perez F. 234 Perez L. A. 103 Okuhara K. 161 Okukado N. 270 281 Padwa A, 112 133 178 239 246 247 Periasamy M. 205 Peringer P. 19 Olah J. A, 208 Paetzold P. 101 Perkins M. J. 90 134 Olah G. A, 65 70 206 208 Pagni R. M. 169 Perkins P. E. 281 209 219 286 Paillous N. 83 Perlin A. S. 16 Oldham P. H. 213 Olive S. 210 Painter G. R. 252 Palazon B. 187 Perret C. 287 Perumal P. T. 221 Oliver S. 63 Pale P. 61 Peruzotti G. 359 Author Index Perz R. 75 Pete J.-P. 61 Peter R. 313 Peters K. S. 137 Petragnani N. 163 Petraitis J. J. 62 192 Petrov A. A, 295 Petrzilka M. 185 Petty C. B. 336 Pez G. P. 255 Pfeffer P.E. 20 Pfeil J. L. 239 Pfleiderer W. 32 Pfriem. S.. 188. 196 Pfund,’R.’A. 198 Philip T. 42 Phillips G. B. 58 Piade J. J. 234 Piau F. 277 Pienta N. J. 155 186 Pieper W. 101 Pierre J.-L. 229 Piers E. 296 Pietraszkiewicz M. 59 345 Pietro W. J. 40 Pike J. E. 351 Pineda N. 87 Ping-Sun Chu 340 Pinkus A. G. 75 Pinnick H. W. 182 Pinson J. 117 Piquard J.-L. 71 Pirkle W. H. 167 Pirrung M. C. 184 313 314 Pitzer R. M. 47 Pizzolato G. 225 Platz M. S. 108 Pletcher D. 117 Plunkett J. J. 261 Podda G. 283 Poirier R. A. 39 43 Poliakoff M. 108 Politzer I. R. 68 Pollack S. K. 45 Pollicino S. 62 Pollini G. P. 371 Poiniaszek R. P. 155 186 Poloni M. 209 Poncher R.384 Ponder J. W. 378 Ponkshe N. K. 249 Ponomareva T. K. 117 Pople J. A, 39 43 44 46 115 285 Porter J. D. 119 Porter N. A, 367 Porzi G. 302 Posner G. H. 168 173 299 Pougny J. R. 290 Poulter C. D. 67 Powell M. 123 Powell M. F. 73 79 Poyser N. 350 Prasad K. 237 Pratt R. F. 246 Presser N. 63 Pressman B. C. 252 Preston P. N. 246 Price L. G. 319 Price P. 359 Price R. T. 58 Principe P. A. 236 Pring G. M. 27 Prinzbach H. 64 Proctor C. J. 5 Probster M. 282 Pross A, 45 Pruskill I. 258 Puar M. S. 342 Puchalski A. E. 138 Pulay P. 40 42 Pulwer M. J. 112 142 Purohit A. K. 252 Purvis G. D. 40 Pye W. E. 333 Quast H. 143 235 242 Quayle P.179 237 239 Quinkert G. 139 Quintard J. P. 281 Quirici M. G. 306 Rabajille E. 393 Rabin B. R. 392 Rabjohn N. 121 Radom L. 45 205 Raghavachari K. 46 Rahimi-Rastgoo S. 249 Rainey D. K. 357 Rajan S.,16 Rajananda V. 8 Rajappa S. 184 Ramalingam K. 211 Raman K. 249 Ramendik G. I. 9 Rammash B. Kh. 55 Rana S. S. 168 299 Rand C. L. 148 270 291 304 Randall M. J. 365 Ranganayakulu K. 69 201 Range G. 87 Rannala E. 32 Rao D. V. 219 Rao V. S.,16 Raw U.,8 Rappe A. K. 40 Rappoport Z. 65 Raston C. L. 223 Ratcliffe R. W. 237 Rathaum M. L. 236 Raucher S.,364 Rauk A, 69 201 Ravichandran R. 102 Ravishankara A. R. 91 Read C. M. 219 Read R. W. 60 Reagan D.R. 165 Rees C. W. 226 244 245 Reetz M. T. 313 Regitz M. 99 113 114 Regondi V. 169 Rei C. 75 Reich H. J. 228 Reich I. L. 228 Reichert C. F. 333 Reichlin D. 55 191 334 Reiffen M. 109 Reinecke M. G. 99 244 Reinhard D. 111 Reinhoudt D. N. 63 Reisenauer H. P. 188 189 196,294 Reiser J. 118 Renaud R. 123 Renk E. B. 88 Rentzea C. N. 248 Reshef D. 275 Rest A. J. 241 Revial G. 194 Rewicki D. 285 Reynolds D. P. 190 357 Rhodes J. 11 Rhouati S.,99 250 Ricard J. 392 Rice J. E. 34 Rich I. D. 295 Richard L. 258 Richards K. E. 208 Richarz. R.. 15 Ri:hey,’H. G.,jun. 287 Richter W. 7 Rickards R. W. 190 358 359 Ridd J. H. 24 206 207 Rideout D.C. 54 Riediker M. 266 306 Rieke R. D. 287 Riera J. 213 Riggs N. V. 210 Rih,. G.. 252 Rimmelin J. 34 36 Rio G. 142 Risley J. M. 22 Rissler K. 232 Rist G. H. 139 Ritzer J. 106 Rivett A. J. 392 Rizzi J. P. 225 Robaugh D. A, 86 Robb M. A. 39 Robbiani C. 334 344 Roberge G. 337 Robert A, 351 Roberts B. P. 84 85 90 Roberts C. 83 Roberts J. D. 16 27 102 Roberts J. S.,375 Roberts R. J. 383 Roberts R. M. 210 410 Roberts S. M. 190 191 347 351 355 356 357 369 374 Robins M. J. 299 Robinson A, 250 Robinson S. R. 206 Robinson W. T. 208 Rodgers M. A. J. 51 Rodini D. J. 58 Rodriguez A. 178 239 Roellgen F. W. 9 12 Roengsumran S. 210 Roessler F.164 296 Rogers D. 87 Rokach J. 243 Rollinson S. W. 175 Romer R. 200 Rondan N. G. 45 52 56 61 103 112 133 203 285 334 Ronlan A, 122 Rooney J. J. 61 Roos B. O. 40 Root K. S. 287 Ros F. 213 Rose R. K. 168 Rosenfeld M. N. 219 Rosenstock. H. M.. 4 Rosenthal R.J. 133 Ross B. C. 237 Rossi R. 306 Rossiter B. E. 168 Roswell D. F. 68 Roth H. D. 108 Rotzoll G. 86 Roullier L. 118 Roumestant M. L. 57 345 Roush W. R. 340 Roussel M. 153 Roux D. 46 Roux-Schmitt M. C. 74 Rowbottom J. D. 121 Rozeboom M. D. 56 334 Rubenstein A. H. 384 Rubin B. 133 Rubin M. B. 63 Ruddlesden J. F. 262 Riichardt C. 87 Riicker C. 299 Riingeler W. 60 186 Ruger W. 202 Rutenberg K.283 Ruiz J. M. 19 Runsink J. 103 Russell G. A, 90 94 Russell P. J. 144 Russell R. A, 98 224 Russell W. 353 Russey W. E. 217 Ruth J. L. 271 Ruth T. J. 216 Rutsch W. 177 Ruzziconi R. 78 Ryabov A. D. 222 Ryan T. M. 11 Rychnovsky S. D. 242 329 Rycroft D. S. 17 75 Rys P. 208 Ryu J. C. 36 Rzepa H. S. 41 49 50 Sabin J. R. 105 Saburi M. 262 Saddler J. C. 360 Saegusa T. 338 Saenger W. 252 Saijo S. 366 Sainsbury M. 123 St. Amour T. E. 17 23 Saito I. 51 Sakakibara T. 150 Sakan K. 177 Sakano K. 226 Sakata J. 73 313 Sakata Y. 150 Sakizadeh K. 213 Sakurai H. 84 135 217 295 Salem L. 46 Salerno G. 269 Salomon R. G. 359 Samal P. W. 41 79 Sammes P.G. 98 219 Samoson A, 26 Sana-Ullah C. 213 Sandall J. P. B. 24 207 214 224 Sandel V. R. 206 Sanders J. K. M. 8 197 Sandmeyer T. 214 Sandri E. 62 Sandri S. 302 San Filippo J. 295 Sanger F. 381 Sannicolo F. 222 Sano H. 306 Santhanam M. 139 Santiago C. M. 61 133 Santikam S. 12 Santini C. 192 Sard H. 62 Sargent R. W. H. 40 Sarkar T. 338 Sasakai Y. 236 Sasaki M. 30 31 35 Sasakura K. 220 Sasson Y. 154 Sastry K. A. R. 152 180 Sato F. 163 259 287 300 SatO K. 53 Sato M. 163 259 270 287 300 Sato T. 271 Sato Y. 174 Satoh S. 127 Satterthwait A. C. 75 Satyamurthy N. 211 Satyanarayana P. 174 Author Index Sauer G. 245 Saunders J. 245 Saunders J.O. 193 Saunders L. C. 362 Saunders M. 69 Sauter H. 64 Savard M. 248 Saveant J. M. 117 Saw P. M. 319 Sawada S. 166 Sawyer J. A, 155 186 Scahill T. A, 236 Scaiano J. C. 87 88 89 109 138 141 Scarborough R. M. 189 Schaad L. J. 44 Schaefer G. 104 186 Schaefer H. F. tert. 39 43 44 47 48 49 110 115 205 Schafer U. 188 Schaub R. E. 351 Scheffer J. R. 197 Scheinmann F. 351 Schenke T. 103 Schepp H. 105 Schiavelli M. D. 261 Schill G. 232 Schilling M. L. M. 108 139 Schillinger W. J. 364 Schipper P. 85 Schlegel H. B. 39 46 Schleiffer E. 36 Schletter I. 375 Schleyer P. von R. 40 41 42 43 44 45 46 66 72 196 200 203 285 Schlosser M. 78 Schmalstieg H.199 Schmid G. 177 Schmidt J. L. 216 Schmidt M. W. 47 Schmidt R. R. 337 Schmierer R. 55 318 334 Schmitt R. 200 Schmitthenner H. F. 339 Schmitz D. 101 Schmitz L. R. 68 Schmuff N. R. 321 Schmulbach C. D. 17 Schneider G. M. 30 Schneider M. 196 Schneider W. P. 351 373 375 Schoeller W. W. 103 Schoen A. E. 12 13 Schonberg A, 138 Schofield K. 207 208 Scholz K.-H. 186 Schomburg D. 252 Schostarez H. 194 Schrauzer G. N. 87 Schreiber S. L. 192 Schreiner J. L. 167 Author Index Schriewer M. 293 Schriver G. W. 45 Schubert H. 113 Schubert K. 85 Schuchardt V. 266 Schiigerl K. 86 Schug J. C. 50 Schulman J. M. 44 Schulten H.-R. 9 Schultz A.G. 102 Schultz P. G. 102 143 Schulz G. 237 Schulz R. 199 Schumburg K. 248 Schuster A, 185 Schuster G. B. 109 Schwartz J. S. 151 266 306 359 Schwartz U. 139 Schwarz H. 3 4 65 Schweig A. 41 199 Schweizer W. B. 198 Schwellnus K. 325 Schwenk A, 19 Sciacovelli O. 148 304 Scolastico C. 171 Secco A. S. 197 Sedgwick R. D. 10 11 Seebach D. 181 250 316 Seeger C. 86 Seeman J. I. 40 Seidel G. 252 Seitz D. E. 296 Seki M. 170 Sekine Y. 229 Sekizaki H. 225 Selim A, 318 Selwyn J. C. 87 Semmelhack M. F. 135 Sen Sharma D. K. 5 Senthilnathan V. P. 108 Sependa G. J. 353 Sera A, 32 Serota S. 172 Sessions R. B. 201 Seyden-Penne J. 74 Shabanowitz J. 11 Shaefer C.G. 137 Shah R. C. 91 Shahrisa A, 144 Shamouilian S. 98 224 Shannon P. V. R. 223 Shapiro J. J. 55 Shapiro M. J. 20 Sharma N. D. 228 Sharma R. 237 Sharma R. P. 59 Sharpless K. B. 168 300 Shaw K. R. 177 302 Shaw R. A, 17 Sheldon B. G. 340 Sheldrick G. M. 249 Shelton S. R. 162 Shen C. C. 205 Shen M. 102 Sheradsky T. 101 Shiao M.-S. 67 Shibasaki M. 164 372 373 376 Shigematsu K. 33 136 252 Shih C. 320 Shih D. H. 237 Shih T.L. 184 308 311 Shimazu K. 135 Shimizu I. 229 Shimonishi Y. 9 Shimp L. A. 286 Shiner C. S. 338 Shingaki T. 101 Shinkai S. 33 136 252 Shipley T. 389 Shirai Y. 242 Shirataki Y. 145 Shishido K. 337 342 Shoham G. 252 Shond T.,151 Shono K.295 Shono T.,118 122 124 125 130 241 Short E. L. 128 211 Shringarpure J. 339 Shudo K. 74 Shvo Y. 275 Sieburth S. McN. 62 192 Siegbahn N. 387 Siegbahn P. E. M. 40 Sieger H. 252 Sih C. J. 359 Silberman J. 295 Silverman B. D. 228 Simmons H. E. tert. 21 194 195 Simmons K. A, 167 Simmons W. 201 Simon J. R. 172 Simonet J. 120 125 128 129 Simoni D. 363 Simpson J. T. 136 Sims. R. 3.. 149 Sinai P. 290 Sindler-Kulyk M. 245 Singh B. P. 69 201 Sinnh H. 80 92 Singh K. 90 Sineh. P.. 71. 168 I. I Singh S. K.,'62 192 Singh S. P. 249 Singleton C. K. 383 Sit S. Y. 149 Sitzmann M. E. 212 Siuta G. J. 351 Sjostrom M. 79 Skell P.S. 86 Skelton B. W. 223 225 Sket B. 215 Skinner G. B. 87 Skinner K. L. 102 Skorochodowa T. 137 231 Skotnicki J. S. 351 Skuballa W. 191 373 Skurat V. E. 9 Sladky F. 19 Sluma H.-D. 109 199 Slusarchyk W. A, 236 Smadja W. 159 Smedley T. A, 40 Smith A. B. tert. 189 330 332 Smith B. V. 134 Smith C. Z. 118 Smith H. O. 383 Smith R. D. 287 Smith R. K. 173 Smith T. W. 206 250 296 Smyth T.A, 208 Smyth-King R. J. 94 Snider B. B. 58 Snitman D. L. 308 Soai K. 171 Sohn J. E. 314 Solano-Muiioz F. 385 Solheim L. P. 393 Solladie G. 184 Sondheimer F. 99 Sonnewald U. 339 Sonoda A, 147 Sonoda N. 139 Sood R. 359 Sooher. D. W.. 128 Soppe-Mbang,'H. 89 Sordo T.205 Sorensen T. S. 68 69 201 Sosonkin I. M. 117 Soulen R. L. 197 Soumillion J. Ph. 134 South M. S. 166 Spaleck W. 140 Speckamp W. N. 327 Speranza M. 68 243 Spiegler W. 76 221 Spinelli D. 212 Spitznagel G. W. 285 Squillacote M. E. 102 Squiller E. P. 287 Srinvasan C. V. 243 Srivastava S. 110 Staab H. A, 229 Stach J. 121 Stadeli W. 16 Stampfli B. 53 Stang P. J. 110 Stange A,,299 Stanney K. 206 Stapersma J. 284 Stark R. E. 25 Staub P. 36 Stauber S. 216 Staunton J. 20 Stawitz J. 242 Steenken S. 89 Steglich W. 247 412 Stein S. E. 86 Stein S. J. 375 Steinbach K. 109 Steinbeck K. 103 112 Steinberg H. 56 Steiner D. F. 384 Steinhoff G.143 Steitz T. A, 388 Stella L. 261 Stenberg V. I. 249 Stenkamp R. E. 388 Stephenson L. M. 58 141 Sterna L. L. 81 Steuber F. W. 242 Stevens J. A, 242 Stevens M. A, 176 Stevens M. F. G. 246 Stewart A, 262 Stewart C. A. 293 Stewart R. F. 40 Still W. C. 177 184 198 297 302 Stillwell R. N. 8 Stirling C. J. M. 78 Stobie A, 168 Stoll R. 12 Stolow R. D. 41 79 Stoodley R. J. 237 Storch W. 18 Stork G. 338 359 364 Stranks D. R. 29 Straub K. M. 9 Straughan B. P. 32 Strauss H. L. 197 Strausser H. R. 351 Streeck H. 225 Streitwieser A,,jun.. 45 50 205 Strich A, 40 Strickland S. M. S. 193 Strijtveen B. 300 Strogov G. N. 117 Strydom P. J. 63 Stubbs M.E. 228 Stuber F. A. 219 Stiitz P. 237 Stuttle K. A. J. 362 Subramanian N. 355 Subramanian P. L. 211 Suda K. 127 Suda M. 186 Sudoh R. 150 Suga K. 111 Sugahara K. 111 Sugahara T. 376 Sugasawa T. 220 Sugawara T. 17 143 Suggs J. W. 108 Sugimoto N. 31 Suginome H. 127 156 306 Sugita S. 122 Sukumaran K. B. 133 224 Sullivan G. R. 27 Sun F. 370 Sunamoto J. 232 Sunday B. R. 342 SunjiC. V. 184 255 Surbeck J. P. 120 Surman D.J. 10 Surzur J.-M. 261 Sustmann R. 83 Susuki K. 38 Sutcliffe L. H. 144 Sutcliffe R. 84 Sutherland I. O. 174 Sutherland J. K. 353 Sutthivaiyakit S. 276 Suzukamo G. 233 300 Suzuki A, 156 273 Suzuki H. 208 337 Suzuki K. 225 243 283 Suzuki N.135 Suzuki R. 159 Suzuki S. 157 Suzuki T. 278 380 Svoronos P. 224 Swaddle T. W. 29 Swanson B. J. 144 Sweeny J. G. 59 Swenton J. S.,121 125 320 Swern D. 101 Syfrig M. A, 250 Sykes R. B. 236 Sylvestre-Panthet,P. 57 345 Sylwester A. P. 102 Symons M. C. R. 201 218 Sypniewski G. 206 Szantay C. 351 363 Szeimies G. 200 Szele I. 214 Szmuszkovicz J. 236 Taba K. M. 206 250 296 Tabakovii I. 126 Tabata A, 158 Taber T. R. 184 308 309 Taft R. W. 24 Takacs J. M. 318 Takada T. 39 Takagi T. 9 Takahashi K. 141 239 242 Takahashi T. 236 325 Takahashi Y. 189 Takai I. 150 Takai K. 61 270 Takakashi M. 233 Takamura N. 113 Takano S. 342 Takasuka M.239 Takata J. 241 Takata T. 234 Takaya H. 167 233 278 Takegami Y. 273 279 Takehira Y. 98 224 Takemura K. H. 34 Taketsuru H. 239 Takeuchi H. 99 Author Index Takeuchi S. 262 Takeuchi T. 355 Takigawa T. 364 Takisawa N. 30 Takundwa C. 269 Taleb-Sahraoui S. 187 Tallec A, 130 Tal’roze V. L. 9 Tamao K. 243 283 Tamaru Y. 159 182 Tamblyn W. H. 112 113 155 275 Tamino A, 380 Tamura C. 237 Tamura M. 233 300 Tamura R. 92 Tamura Y. 59 249 Tanaka M. 272 Tanaka T. 303 359 Tane J. P. 188 Tang P. W. 229 Taniguchi H. 269 Taniguchi I. 123 Taniguchi Y. 38 Tanimoto M. 155 Tanimoto Y. 87 Tanneburg H. 129 Tanner D. 231 Tanner D. D. 93 Tantrarant T.217 Tarasov V. F. 81 Tarchini C. 78 Tarnchompoo B. 161 Tarnowski B. 250 Tasaka M. 205 Tashiro M. 219 244 Tatsmami S. 385 Tawfik A. E. M. 114 Taylor B. S. F. 215 Taylor D. R. 249 Taylor G. A. 219 Taylor G. F. 336 Taylor L. C. E. 12 Taylor P. G. 208 Taylor P. W. 223 Taylor R. 225 Taylor R. J. K. 362 Taylor S. K. 283 Tebbe K. F. 297 Tedder J. 206 Tedder J. M. 80 92 Tegmo-Larsson I.-M. 56 334 Teller G. 8 Temple J. S. 151 266 306 Tennant G. 246 Teranishi S. 275 Terashima S. 359 Terlouw J. K. 3 Tetler L. W. 11 Teyssie P. 114 217 Tezuka T. 61 133 218 Thac T. D. 88 Thea S. 76 Author Index 413 Thebtaranonth Y. 161 Theis C. H. 246 Thiel W.41 Tsai Y.-M. 327 Tsoi S. C. 245 Tsubata. K.. 124. 241 Van Humbeeck L.. 351 van Hummel G. J. 63 van Koten G. 283 Thind S. S. 213 Thoennes D. 285 Thom I. G. 307 Thomas J. M. 26 Thompson D. W. 261 Thompson J. L. 373 Thompson R. L. 91 Thulin. B. 230 231 Tilak B. D. 252 Tilley J. W. 220 Tipton K. F. 392 Tissot P. 120 Tius M. A, 223 Tobe Y. 62 227 Tobinaga S. 122 Tochtermann W. 222 Toder B. H. 332 Totsch W. 19 Togasi M. 39 Toi H. 147 Tokuda M. 127 Tolbert L. M. 52 Tsuboi M.,'42 ' Tsuchihashi G. 359 Tsuji J. 157 189 255 265 325 Tucker J. R. 104,186 Tuddenham D. 226 Tulich L. 154 Tully F. P. 91 Turdivel R. 126 Turner E. S. 134 Turner J. J. 108 Turner J. V. 330 Turro N. J. 47 81 87 133 Tyler A. N. 10 11 Tyrell A. W. R. 367 Tysban A. V. 162 Tzeng D. 115 292 Tzidony E. 4 141 Ucciani E. 243 van Kruchten E.M. G. A. van Leusen D. 113 155 Van Meerssche M.,190 353 Vannes P. 190 353 Vanni H. 30 van Wallendael S.. 263 Van Willigen H. 25 Varma M. 78 Vasilvitskaya E. M. 30 Vasudevan S. 26 Vasyute Y. V. 9 Vazeux M. 194 Vederas J. C. 21 Veith H. J. 9 Venit J. 180 Venugopalan B. 237 Verhoeven J. W. 56 Vermeer P. 283 Vesnovskaya G.I. 81 Vestal M. L. 12 Vetter W. 232 70,201 Tom T. 359 Uchida T. 35 Vickerman J. C. 10 11 Tomis M. 251 Uda H. 189 Vidal S. 215 Tomasin A, 205 Uemura S. 150 158 Viele C. 129 Tomaszewski J. E. 227 Ueno A, 141 Viers J. W. 50 Tombo G. M. R. 198 Tomioka H. 114 Ueno Y. 306 Ueoka T. 197 Vikingur E. G. 224 Vincent E. J. 19 Tomita K. 331 Tomita M. 174 Tomizawa K. 218 Tonachini G. 40 Tongpenyai N. 276 Uhm S. T. 287 Uike Y. 97 Ujjainwalla M. 160 Ulrich P.378 Umehara Y. 138 206 Viscogliosi L. A. 221 Vittinghoff K. 71 Vodar. B.. 30 Vogtle' F.;229 230 231 252 Volkel G. 28 Torgerson D. F. 10 Torgerson P. M. 31 Torii S. 127 Torisawa Y. 373 Tortorella S. 130 Toshimitsu. A,. 150 Townson M.,82 215 Toya T. 232 Toyoda T. 220 Traficante D. D. 17 Tran Dinh An 78 Traverso P. G. 205 Trayer I. P. 392 Trejo W. H. 236 Trill H. 83 Trinquier G. 43 Trippett S. 183 Trius A, 264 267 Trocha-Grimshaw J. 225 Troll T. 127 Troostwijk C. B. 170 252 Trost. B. M.. 47. 55. 191. 194,264,265; 299,32i 324 Trotter J. 197 Trueblood K. N. 252 Tsai C. S. 391 Tsai D. I. S. 307 Umo K. 380 Uneyarna K. 127 Unger S.E. 10 11 13 Untch K.G. 359 UskokoviC M. R. 57 342 Usmani A. A, 341 Utamapanya S. 161 Utimoto K. 276 Utley J. H. P. 117 118 128 Valentine B. 17 Valentine D.jun. 220 Valentine K. M. 20 Valery J. M. 159 Van der Beeke P.,33 34 van der Kook H. O. 293 van der Saal W. 242 Van Derveer D. 184 308 Vane J. R. 350 35 1 Van Eldik R. 30 Van Epp J. E. jun. 227 Van Etten R. L. 22 Van Haverbeke Y. 7 van Horn D. E. 148,291 Van Horn D. L..270 314 304 Voet J. G. 389 Vogel E. 184 308 309 Vogel P. 53 Volkel. G..32 Vollhardt,'K. P. C. 188 210 Vollmann H. 225 Von Philipsborn W. 16 19 260 274 Von Sprecher G.,200 Vorbruggen H. 191 Vorpagel E. R. 50,205 Voss J. 128 Vrieze K. 283 Vuper M. 295 Waali E.E. 44 109 199 Wada F. 220 Wada M. 366 Waddilove R. A, 24 Waddington T. 22 Wadsworth A. H. 357 Wadsworth D. H. 161 Wadt W. R. 40 Wagner P. J. 138 Wagner W. 6 Wahrhaftig A. L. 4 Wakabayashi 363 Wakamatsu S. 144 Wakatsuka H. 355 Wake S.100 Wakefield B. J. 191 369 Waldner A, 200 Waley S. G. 384 Walker A, 179 239 Walker G. E. 69 Walker J. 214 Wallach O. 216 Wallenfels K. 118 Wallenstein M. B. 4 Wallis C. J. 368 Walpole A. L. 353 Walsh E. 169 Walton J. C. 83 92 Walton T. E. 147 Wamhoff H. 127,246,247 Wang A. 66 Wang C.-L. J. 364 Wang H. K. 273 Wang J. T. 83 Wang Y.-F. 179 Ward D. E. 177 Ward R. S. 174 Warin R. 114 217 Warkentin J. 106 147 Warren C. T. 77 Warren S. 149 176 304 Warrener R. N. 98 224 Warshel A, 41 Warwick P. 271 Wasserman H. H. 51 142 Wassermann M. 350 Watanabe H. 229 279 300 Watanabe K. 279 Watanabe S. 111 Watanabe T. 125 Watanabe Y. 179 279 Waters D. N. 210 Watkins M.I. 206 Watson T. W. 75 Wattanasin S. 219 Watts. W. E.. 211 Wautyer H,ii- ~ Webb C. F. 190 357 Webb R. R. 59 345 Weber A, 118 Weber G. 31 Weber R. 17 Weber W. 60 Weber. W.-D.. 139 Weber; W. P.,’ll5 292 Weed G. C. 87 Wege D. 97 241 Weinreb S. M.,286 339 Weiss E. 285 Weiss M. J. 351 Weissman S. 383 Weissmann C. 384 Weismann G. R. 170 Weitz E. 63 Weller T. 316 Wells J. S. 236 Wells P. B. 275 Wells R. D. 383 Wender P. A. 56 62 192 243 319 Wendt H. 130 Wenkert D. 252 Wenkert E. 114 Wennerstrom O. 231 Wermeckes B. 286 Werner G. 121 Werner P. 249 West P. R. 99 West R. 43 114 294 295 Westheimer F. H. 75 Wetter W. P. 107 Weyerstahl P.11 1 Whalley E. 30 Wharry S. M. 16 White A. H. 223 225 White A. W. 243 White C. T. 184 308 314 White E. H. 68 196 White J. D. 340 White M. R. 110 White R. F. M. 15 White S. 170 317 318 Whitesell J. K. 286 Whiteside R. A. 39 46 Whitesides G. M. 287 Whitham G. H. 248 Whitlock B. J. 232 Whitlock H. W. 232 Whitman D. 206 Whitney R. A, 186 Whittaker N. 365 Whittall J. 63 Whitten C. E. 173 Whyman R. 275 Wiaux-Zamar C. 190 353 Wiberg K. B. 62 196 Wieber M. 281 Wiebers J. L. 12 Wiering P. G. 56 Wiggins P. L. 67 Wijnberg B. P. 327 Wilby A. H. 148 Wilkins C. L. 8 Will J. P. 228 Wille S. 16 Willen B. H. 103 Williams A. 76 184 Williams D.H. 5 7 8 12 Williams D. J. 226 Williams D. R. 149 170 317 318 Williams E. 364 Williams F. 83 Williams G. H. 91 213 214 215 224 Williams G. M. 228 Williams J. C. jun. 51 61 133 Williams J. R. 41 Williams P. D. 241 Author Index Williams P. S. 87 Williams R. K. 31 Williams R. V. 335 Willis A. C. 197 Willis B. J. 192 325 Willis J. P. 122 Wilson C. H. 369 Wilson C. J. 31 Wilson J. S. 299 Wilt J. W. 90 Winans R. E. 216 Wine P. H. 91 Winter R. E. K. 196 Winter W. 137 231 Wintermayr H. 202 Wirth D. J. 54 Wirth D. D. 93 191 334 Wirthlin T. 15 Wirz J. 199 Witholt B. 168 Wittig G. 143 Wojciechowski P. S. 34 Wold S. 79 Wolfe J. F. 213 Wolfe. S..46. 153 Wolff,’S.,’141 196 Wolff T. 136 Wolstenholme J. 11 Wolters J. 293 Wong A. K. 169 Wone. H. N. C.. 99 Won;; J. L. 55’ Wong P. C. 109 Wong S. K. 87 88 Wong Y.-F. 197 Wood D. L. 43 115 294 Wood J. M. 86 Woodard S. S. 168 300 Woodgate P. D. 114 Woodthorpe K. L. 102 Woodward R. B. 177 252 Woolfson R. 385 Woolley G. T. 190 191 355 356 369 Wootton G. 367 Worthington P. 275 Wovkulich P. M. 57 342 Woynar H. 88 Wrackmeyer B. 18 Wray V. 15 Wright C. W. 109 Wright J. J. 342 Wubbels G. G. 87 141 Wurthwein E. U. 43 Wynberg H. 168 Wynn S. 174 Xu R. X. 243 Yabushita S. 51 Yagi H. 227 228 Yago N. 385 Author Index 415 Yagoub A. K. 250 Yamabe S.39 Yamada H. 32 Yamada M. 170 331 Yamada N. 251 Yamada S. 359 Yamada Y. 138 206 300 Yamaguchi H. 123 150 Yamaguchi K. 51 Yamaguchi Y. 39 49 Yamakado Y. 165 307 Yamame S. 125 Yamamoto H. 165 292 307 333 Yamamoto K. 157 232 Yamamoto Y. 147 177 184 311 313 315 Yamamura S. 123 Yamanda Y. 168 Yamashita M. 359 Yamashita Y. 53 157 Yamauchi M. 125 Yamazaki C. 249 Yamazaki H. 272 Yamazaki N. 170 Yamazaki T. 236 Yannoni C. S. 26 71 Yano S. 155 Yasmenko A. I. 38 Yasuda A, 233 Yasuda H. 153 259 260 Yasuda M. 135 217 Yasuda T. 127 Yasukouchi K. 123 Yatagai H. 184 313 315 Yates J. B. 59 345 Yatsimirsky A. K. 222 Yergey A. L. 12 Yeung D. W.K. 147 Yijima C. 127 Yip R. W. 84 Yoh S. 36 Yokoe I. 145 Yokota K. I. 266 281 Yokoyama Y. 364 Yonemitsu T. 19 Yoshida J. 155 Yoshida M. 214 225 Yoshida T. 162 239 290 Yoshida Z. 159 182 Yoshidomi M. 269 Yoshifuji M. 250 Yoshihiro M. 118 Yoshikawa S. 262 Yoshikawa Y. 226 Yoshimine M. 83 Yoshimura J. 262 Yoshino S. 56 Yoshioka H. 180 Yoshioka Y. 43 115 Yoshiya H. 219 Yoshizawa S. 128 Young C. M. 103 Young D. W. 252 Young S. D. 113 184 314 Young S. N. 357 Yu M. 332 Yuan R.,382 Yuh Y. 42 Yuki H. 167 Yus M. 151 152 284 289 Zabeau M. 383 Zajdel W. J. 45 Zaugorodnii V. S. 295 Zawadzki S. 152 Zbaida D. 101 Zdunek L. Z. 23 Zeiss H.-J. 184 Zhulin M.30 Zimmer. 0.. 63 Zipkin R. E.,331 Zirngibl U. 196 Zoch H.-G. 200 Zoeckler M. T. 62 Zollinger H. 214 222 Zolotoi N. B. 9 Zon,G. 100 296 Zoran A, 154 Zoretic P. A, 366 zucco c.,75 Zupan M. 215 216 Zupancic J. J. 109 Zwaard A. W. 202 Zwanenburg B. 189 Zweifel G. 149 300 304 Zwierzak A, 152 Zwinselman J. J. 9

ISSN:0069-3030    

DOI:10.1039/OC9817800395

出版商:RSC    

年代:1981

数据来源: RSC