年代:1970 |
|
|
Volume 2 issue 1‐4
|
|
1. |
AMINO ACID COMPOSITIONS and N‐TERMINAL AMINO ACIDS OF ALL THE TRYPTIC PEPTIDES FROM THE α and β POLYPEPTIDE CHAINS OF ADULT HEMOGLOBIN OF THE RHESUS MONKEY (Macaca mulatto) |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 1-12
Genji Matsuda,
Tetsuo Maita,
Hiroshi Take,
Preview
|
PDF (702KB)
|
|
摘要:
Globin prepared from adult hemoglobin of the rhesus monkey was separated into α and β polypeptide chains by the countercurrent distribution method. The α and β polypeptide chains were digested with trypsin. All the tryptic peptides were isolated and purified by column and paper chromatography. The amino acid compositions and the N‐terminal amino acid of these tryptic peptides were analyzed.According to the results thus obtained, the α and β polypeptide chains of adult hemoglobin of the rhesus monkey are respectively composed of 141 and 146 amino acid residues just as those of human hemoglobin. However, it is presumed that there exist at least four amino acid substitutions in the a polypeptide chain and eight in the β polypepti
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01655.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
2. |
AMINO ACID SEQUENCES OF ALL THE TRYPTIC PEPTIDES FROM THE α POLYPEPTIDE CHAIN OF ADULT HEMOGLOBIN OF THE RHESUS MONKEY (Macaca mulatto) |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 13-26
Genji Matsuda,
Tetsuo Maita,
Nagatoshi Igawa,
Hisahiro Ota,
Takao Miyauchi,
Preview
|
PDF (812KB)
|
|
摘要:
The a polypeptide chain of adult hemoglobin of the rhesus monkey was digested with trypsin. All the tryptic peptides thus obtained were isolated and purified by column and paper chromatography and amino acid sequence analyses of these peptides were performed mainly by partial hydrolyses with enzymes, the DNP method, and the PTC method. The comparison of the results with the known sequences of the corresponding peptides from the a polypeptide chain of human hemoglobin showed that there were four differences in amino acid sequences of these peptides between rhesus monkey and humans.
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01656.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
3. |
ISOLATION and CHARACTERIZATION OF PEPTIDES PRODUCED BY THE MILD ACID HYDROLYSIS OF BOVINE SUBMAXILLARY MUCIN* |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 27-36
Fred Downs,
Ward Pigman,
Preview
|
PDF (632KB)
|
|
摘要:
The rate of release of amino acids during partial acid hydrolysis of bovine submaxillary mucin has been studied. A number of di‐ and tripeptides have been isolated on the amino acid analyzer. Three β‐hydroxyamino acid peptides, Thr‐Thr‐Thr, Ser‐Ser, and Thr‐Ser have been isolated and account for 12 % of these amino acids in native mucin. A substantial amount of the glycine and alanine has been isolated as dipeptides of serine and threonine with the fihydroxyamino acids in the amino‐terminal position. Proline, valine, isoleucine, and leucine seem to be in close association in the peptide core. The same pattern of peptides has been obtained from the partial acid hydrolysis of ovine subm
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01657.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
4. |
STUDIES ON THE CONFORMATION OF AMINO ACIDS* |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 37-45
P. K. Ponnuswamy,
V. Sasisekharan,
Preview
|
PDF (603KB)
|
|
摘要:
In this paper, the results of the potential energy calculations on the conformations of some amino acids are given. The non‐bonded, electrostatic, and torsional contributions to the total energy of the molecule were calculated using appropriate functions and their role in predicting the conformation of amino acids is discussed. It is shown that electrostatic interaction between the amino group and the carboxyl group is mainly responsible for the plane of the carboxyl group to be coplanar with the plane through N, Cα, andC1atoms. It is also shown that the presence of a γ‐atom in position II necessiates a large deviation from the coplanarity between the carboxyl plane and the N, Cα, C plane.The results indicate that the backbone conformations of all the amino acids are nearly the same and could be shown to be the same as those of glycine and alanine. Also, the theoretically predicted conformations about the Cα‐Cβbond in aminobutyric acid could explain the observed γ‐atom positions in all th
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01658.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
5. |
STUDIES ON THE CONFORMATION OF AMINO ACIDS |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 47-57
P. K. Ponnuswamy,
V. Sasisekharan,
Preview
|
PDF (540KB)
|
|
摘要:
Potential energy calculations were carried out to determine the possible conformations of N‐ and C‐terminal glycyl and alanyl residues. Non‐bonded and electrostatic contributions to the conformational energies were obtained and their role in predicting the favourable conformations has been assessed. It is shown that in the case of glycyl and alanyl N‐terminal residues, a conformation in which the plane of the amide group is nearly coplanar with the plane through the backbone atoms N, C, andCis the most favourable one and this conformation is mainly stabilized by the electrostatic interactions. The results also indicate that the backbone conformation of all the N‐terminal residues with various side chains are nearly the same and could be shown to be that of glycyl and alanyl N‐terminal residues. The importance of the coplanarity of the amide and the carboxyl groups and so also their perpendicular orientation in the C‐terminal residue
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01659.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
6. |
SYNTHESIS and PROPERTIES OF ARGININE OLIGOPEPTIDES |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 59-65
Hisashi Ito,
Iwao Ichikizaki,
Toshio Ando,
Preview
|
PDF (485KB)
|
|
摘要:
Di‐, tri‐, and tetra‐arginine were prepared from carbobenzoxy‐nitro‐L‐arginine via carbobenzoxy‐nitro‐L‐arginyl‐nitro‐L‐arginine methyl ester, carbobenzoxy‐nitro‐L‐arginyl‐nitro‐L‐arginyl‐nitro‐L‐arginine methyl ester, and carbobenzoxy‐nitro‐L‐argi‐nyl‐nitro‐L‐arginyl‐nitro‐L‐arginyl‐nitro‐L‐arginine methyl ester, respectively, by mixed anhydride and dicyclohexyl‐carbodiimide (DCC) methods. Measurement of the optical rotation of the peptide hydrolysates at 224 mμ showed that no racemization has occurred during the syntheses. Mean residue rotations at 224 mμ of these peptides have some relationship with the chain length. Color values of the Sakaguchi reaction per
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01660.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
7. |
SULFENYL HALIDES AS MODIFYING REAGENTS FOR POLYPEPTIDES and PROTEINS |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 67-74
Francesco M. Veronese,
Enrico Boccä,
Angelo Fontana,
Preview
|
PDF (514KB)
|
|
摘要:
A new method is described for the inter‐ and intramolecular cross‐linking of the tryptophan residues in polypeptides and proteins. The reaction employed involves treatment of the tryptophan‐containing derivative with 2,4‐dinitro‐1,5‐phenyldisulfenyl chloride (DNPDS‐Cl)* in acidic media. This bifunctional sulfenyl halide reacts selectively with two molecules of tryptophan at the position of indole nucleus, leading to a cross‐linked compound. The only other amino acid affected is cysteine, which similarly can be cross‐linked through formation of mixed disulfide bonds. The reaction with the thiol function of cysteine can be reversed by reduction with mercaptans, allowing selective cross‐linking of tryptophan residues.In order to test the effectiveness of the method, several tryptophan derivatives were cross‐linked by reaction with DNPDS‐Cl in acetic or formic acid, including short sequences of the pancreatic hormone glucagon and gastrin.The reaction was also applied to glucagon, in which case the single tryptophan residue was reacted with the reagent and the dimer isolat
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01661.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
8. |
STUDIES ON BACTERIAL PROTEASES |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 75-81
D. Tsuru,
T. Yoshimoto,
H. Yoshida,
H. Kira,
J. Fukumoto,
Preview
|
PDF (449KB)
|
|
摘要:
Amino acid composition of neutral protease obtained from the culture broth o/Bacillus subtilis var. amylosacchariticus was dertermined. The enzyme was composed of 308 residues of amino acids: Lys15His5, Arg9Asp43, Thr31, Ser30, Glu23, Pro11,Gly27, Ala27, Cys0, Val16, Met2, He12, Leu22., Tyr23, Phe9, Trp3, and amide‐ammonia32on a basis of molecular weight of 34,000. Of 23 residues of tyrosine, 15 groups were found to be normally ionized with the apparent pK value of 10.0, whereas the remainder was ionized only after irreversible unmasking of the tyrosyi residues at higher pH with the pK value of about 12.2. The optical rotatory dispersion measurements showed that [a]D, a0, b0, and Lc were –28, –129, –173, and 276 m/μ, respectively, suggesting the enzyme to contain less than 30 % of α‐helix structure. The negative minimum of the Cotton effect lay at 233 m/μ with the [m] va
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01662.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
9. |
AMINO ACID SEQUENCE IN ALL THE TRYPTIC PEPTIDES FROM THE β POLYPEPTIDE CHAIN OF ADULT HEMOGLOBIN OF THE RHESUS MONKEY (Macaca mulatta) |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 83-97
Genji Matsuda,
Tetsuo Maita,
Masato Yamaguchi,
Masaharu Migita,
Preview
|
PDF (862KB)
|
|
摘要:
The β polypeptide chain of adult hemoglobin prepared from the rhesus monkey(Macaca mulatta)was digested with trypsin. All the tryptic peptides thus obtained were isolated and purified by column chromatography and paper chromatography, and then the amino acid sequence in these peptides was determined. Comparisons of the results with the known sequences of the corresponding peptides from adult human hemoglobin showed there were differences at eight positions in the amino acid sequences of the seven peptides
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01663.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
10. |
THE PRIMARY STRUCTURE OF THE α and β POLYPEPTIDE CHAINS OF ADULT HEMOGLOBIN OF THE RHESUS MONKEY (Macaca mulatto) |
|
International Journal of Protein Research,
Volume 2,
Issue 1‐4,
1970,
Page 99-108
Genji Matsuda,
Tktsuo Maita,
Hisahiro Ota,
Hiroshi Takei,
Preview
|
PDF (544KB)
|
|
摘要:
Countercurrent distribution separated rhesus monkey hemoglobin into α and β polypeptide chains, which were respectively oxidized with performic acid, dissolved in 8 M urea to be denatured at 60° for 45 min, and then digested with pepsin at 37° for 2 hours. Peptic peptides thus obtained from each polypeptide chain were isolated and purified by column‐ and by paper chromatography, and the amino acid composition of each peptide was analyzed. Sequence analysis was carried out by using PTC and DNP methods, if necessary.From the results thus obtained, the present authors established the primary structure of rhesus monkey hemoglobin, taking account of the amino acid sequence in all the tryptic peptides from the α and β polypeptide chains previously r
ISSN:0020-7551
DOI:10.1111/j.1399-3011.1970.tb01664.x
出版商:Blackwell Publishing Ltd
年代:1970
数据来源: WILEY
|
|