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1. |
Immunological analysis of lipophorin in the haemolymph, ovaries, and testes of the fall webworm,Hyphantria cunea(Drury) |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 153-167
Hwa Kyung Yun,
Woo Kap Kim,
Hak R. Kim,
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摘要:
AbstractLipophorin (LP) was purified from haemolymph in last instar larvae ofHyphantria cunea(Drury) by KBr density gradient ultracentrifugation and gel filtration. LP is composed of Apo‐LP I and Apo‐LP II with molecular weights of 230 kDa and 80 kDa, respectively.The level of haemolymph LP in early pupae was somewhat greater than in last instar larvae. In males, this LP concentration is maintained throughout pupal development, whereas the level of haemolymph LP decreases in female pupae beginning at day 7, coincident with the onset of vitellogenesis in the fall webworm. In both male and female adults, haemolymph LP concentrations were dramatically increased in comparison to their pre‐adult levels. Actually, LP was found in the ovary by immunodiffusion, tandem‐crossed immunoelectrophoresis, and Western blotting. Location of LP in the ovary was also traced by immunogold labelling. Also, LP appeared in small amounts in protein yolk bodies of the ovary at an early stage of vitellogenesis, when nurse cells are bigger than the oocyte, but in greater amounts at those stages when the oocyte is larger than nurse cells—that is, when vitellogenesis is actively taking place. This fact clearly reveals that LP is synthesized by fat body and released into the haemolymph, and then taken up by the growing ovary during vitellogenesis. Also, LP was detected in testes by immunological analysis. Western blotting showed that LP was present in testicular fluid but not in the peritoneal sheath and cysts. To test whether LP is also synthesized in testes, testes and fat body tissues were cultured in vitro, indicating that fat body synthsizes LP but testes do not. The result showed that the haemolymph LP itself is taken up into the testes. © 1994 Wiley
ISSN:0739-4462
DOI:10.1002/arch.940270302
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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2. |
Molecular cloning of aDrosophila melanogastergene coding for an homologue of human carboxypeptidase E |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 169-178
Paul Bernasconi,
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摘要:
AbstractPCR primers derived from two functional domains of vertebrate carboxypeptidase E (CPE) were used to generate a probe for screening a size‐selectedDrosophila melanogastergenomic library. A sequence representing about 50% of the expected complete sequence was obtained by translation of the two open reading frames present on a 1.6 kb DNA genomic fragment. This partial sequence, homologous to human CPE, CPM, and CPN, contained the conserved arginine and zinc binding domains. Similarities to the human enzymes were found with stretches that were equally divergent from the three vertebrate carboxypeptidases. Northern blot analysis revealed the presence of a 6.9 kb transcript for this gene inDrosophilaembryos. I postulate that insects possess a single protein fulfilling CPE, CPM, and CPN functions. © 1994 Wiley‐Liss,
ISSN:0739-4462
DOI:10.1002/arch.940270303
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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3. |
“Reduced appendage”: A mutation affecting development of pupal and adult appendages of the moth,Plodia interpunctella |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 179-191
Paul D. Shirk,
Karen L. Ogren,
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摘要:
AbstractA mutant that results in the reduced length of pupal and adult appendages was isolated from a laboratory colony of the Indianmeal moth,Plodia interpunctella(Hübner). “Reduced appendage” (rda) was determined to be an autosomal recessive mutation that affects the development of pupal and adult appendages during the larval/pupal molt. Therdamutation had no observed effect on the larval phenotype. After pupation, the appendages ofrdawere reduced in size as compared with wild‐type. In addition, unsclerotized cuticle underlying the pupal appendages was exposed and the establishment of the boundary between the unsclerotized and sclerotized pupal abdominal cuticle appeared normal even though the imaginal discs ofrdadid not evaginate normally. This demonstrates thatrdaaffects only imaginal discs and that the morphogenesis of structures that were not derived from the imaginal discs were not dependent on interactions with evagination of imaginal discs. Although therdaphenotype resulted in shorter antennae, mouth parts, legs, and wings in pupae and adults, the mutation did not affect the number of cells comprising the imaginal discs or the pupal appendages. Cell counts showed that forewing imaginal discs and pupal forewings from therdamutants contained the same number of cells as did the imaginal discs and wings from the wild‐type strain. Thus,rdaappears to affect processes related to disc evagination and not cell proliferation. © 1994 Wiley‐Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States
ISSN:0739-4462
DOI:10.1002/arch.940270304
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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4. |
Purification and characterization of theManduca sextaneuropeptide processing enzyme carboxypeptidase E |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 193-203
Tracey E. Stone,
Jorge P. Li,
Paul Bernasconi,
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摘要:
AbstractThe neuropeptide processing enzyme carboxypeptidase E (CPE) (E.C.3.4.17.10) has been well studied in vertebrates but its presence in invertebrates has not yet been reported. CPE activity in insects is present in membrane‐bound and soluble forms. The soluble CPE has been purified to homogeneity from the brain of the tobacco hornwormManduca sexta.It is a 57 kDa glycoprotein containing 9% sugars. It is activated 9.2 ± 1.8 fold by CoCl2and inhibited by chelating agents. Its sensitivity to guanidinoethyl‐mercaptosuccinic acid, and its molecular mass, make this enzyme a good candidate to be the insect equivalent of the mammalian CPE. Furthermore, its lack of sensitivity towardsp‐(chloromercuri)benzenesulfonate puts it closer to the vertebrate carboxypeptidase M (CPM). We postulate that insects may possess a single protein fulfilling both CPE and CPM functions. © 1994 Wiley‐
ISSN:0739-4462
DOI:10.1002/arch.940270305
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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5. |
Cytochrome b5involvement in cytochrome P450 monooxygenase activities in house fly microsomes |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 205-216
Minli Zhang,
Jeffrey G. Scott,
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摘要:
AbstractThe involvement of cytochrome b5in different cytochrome P450 monooxygenase and palmitoyl CoA desaturase activities in microsomes from insecticide‐resistant (LPR) house flies was determined using a specific polyclonal antiserum developed against house fly cytochrome b5. Anti‐b5antiserum inhibited the reduction of cytochrome b5by NADH‐cytochrome b5reductase. The antiserum also inhibited palmitoyl CoA desaturase, methoxycoumarin‐O‐demethylase (MCOD), ethoxycoumarin‐O‐deethylase (ECOD), and benzo[a]pyrene hydroxylase (aromatic hydrocarbon hydroxylase, AHH) activities. However, methoxyresorufin‐O‐demethylase (MROD) and ethoxyresorufin‐O‐deethy‐lase (EROD) activities were not affected by this antiserum. These results demonstrate that cytochrome b5is involved in fatty acyl CoA desaturase activities and in certain cytochrome P450 monooxygenase activities (i.e., MCOD, ECOD, and AHH) in LPR house fly microsomes. Other cytochrome P450 monooxygenase activities (i.e., MROD and EROD) may not require cytochrome b5. The results suggest that cytochrome b5involvement with cytochrome P450 monooxygenase activities is dependent upon the cytochrome P450 isoform involved.
ISSN:0739-4462
DOI:10.1002/arch.940270306
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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6. |
Synthesis and deposition of PCG‐100, the main pupal cuticle glycoprotein of the medflyCeratitis capitata |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page 217-234
Graciela L. Boccaccio,
Luis A. Quesada‐Allué,
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摘要:
AbstractWe have studied the developmental expression of the main pupal cuticle glycoprotein, PCG‐100, in the MedflyCeratitis capitata. A polyclonal antiserum was raised against this protein. Western blotting analysis showed that this glycoprotein is integument‐ and stage‐specific. No PCG‐100 or immunologically related polypeptides were detected in other tissues or instars. As studied by microinjection of [35S]methionine in individual flies, in vivo synthesis and deposition of PCG‐100 begins approximately 48 h after the onset of pupariation, shortly after the time of head eversion. Synthesis is maximal at 54–64 h, decreases at 72 h, and practically ceases in fully shaped 4‐day‐old pupae. The time required for PCG‐100 deposition into the cuticle was found to be less than 10 min after its synthesis. This is the first time such in vivo analysis has been performed. © 19
ISSN:0739-4462
DOI:10.1002/arch.940270307
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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7. |
Masthead |
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Archives of Insect Biochemistry and Physiology,
Volume 27,
Issue 3,
1994,
Page -
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ISSN:0739-4462
DOI:10.1002/arch.940270301
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1994
数据来源: WILEY
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