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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (5)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 55-72 
    ISSN: 0739-4462
    Keywords: riboflavin ; serum protein ; protein structure ; waxmoth ; development ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The 85K storage protein that accumulates in the hemolymph of Galleria mellonella during the final larval instar was isolated and purified from newly molted pupae. The separation of fresh hemolymph proteins from larvae or pupae by different chromatographic and electrophoretic procedures indicated the native protein had a Mr of 170,000 and consisted of two identical 85K subunits. Crosslinking experiments using fresh hemolymph followed by Western blotting also indicated a dimeric structure for the native protein. Analyses of the dimer purified from pupal hemolymph indicated that 85K was a glycoprotein, containing approximately 6.5% neutral sugar and about 1.9% amino sugar. Like other insect flavin-binding proteins, 85K has a relatively high histidine content but an uncharacteristically high arginine content. The purified 85K dimer did not bind riboflavin, suggesting that the integrity of the molecule had been altered during purification. However, 85K purified in low yield by Affi-Gel Blue chromatography, did bind riboflavin, indicating that under certain, undefined conditions the functional integrity of the protein could be retained during purification. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
    Additional Material: 11 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 363-380 
    ISSN: 0739-4462
    Keywords: Heliothis ; hybrid male sterility ; mitochondria ; protein synthesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The mitochondrial proteins synthesized by spermatogenic cells from Heliothis virescens, H. subflexa, and their male-sterile backcross progeny were analyzed by using two-dimensional gel electrophoresis. This subset of total cellular proteins was defined by using a combination of cellular fractionation techniques and pulse-labeling in the presence of antibiotics. Mitochondrial morphology was also evaluated in cells from fertile and sterile testes by using the laser dye rhodamine 123. These studies revealed that while abnormal mitochondrial structures are apparent in sperm from backcross moths, neither protein synthesis nor import into the organelle was affected in these individuals. Two mitochondrial proteins exhibiting charge variation between the two parental hybridizing species have been identified, and these results are discussed within the context of a hypothesis developed to account for the sterility phenomenon.
    Additional Material: 8 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 14 (1990), S. 131-150 
    ISSN: 0739-4462
    Keywords: hemolymph ; plasma proteins ; cDNA clones ; DNA sequencing ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Three abundant storage proteins have been detected in larval and pupal hemolymph and pupal fat body of the tobacco budworm, Heliothis virescens. These polypeptides have subunit molecular weights of 74,000, 76,000, and 82,000, as determined by SDS-PAGE and exit as 450,000-Mr hexamers in their native state. A purified 82,000-Mr storage protein fraction has been obtained along with a preparation containing equivalent amounts of the 74,000-Mr and 76,000-Mr subunits, and antisera raised to each of these components have been used to document the developmental profiles of protein accumulation and synthesis by fat body. cDNA clones corresponding to each of three abundant classes of fat body mRNAs have been recovered, and at least one of these has been unambiguously demonstrated to encode the 82,000-Mr storage protein subunit. Northern blot studies with these cDNA clones revealed that the developmental accumulation of transcripts in fat body for each was consistent with the general pattern of storage protein biosynthesis, and more interestingly, that transcirpts hybridizing to two of these cDNA sequences are also found in testes. These two cDNA have also been sequenced revealing that one encodes a polypeptide similar to arylphorins, a class of storage proteins widely distributed in Insecta. The derived amino sequence of the second cDNA, corresponding to the 82,000-Mr protein, had no unusual compositional features and determination of its structural relationship to other hemolymph polypeptides awaits molecular analysis of related genes from other insects.
    Additional Material: 11 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 14 (1990), S. 151-170 
    ISSN: 0739-4462
    Keywords: testis sheath ; gene expression ; protein transport ; spermatids ; mitochondria ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The synthesis of two storage protein subunits, 76,000-Mr and 82,000-Mr polypeptides, by the testes sheath has been studied in Heliothis virescens. Like fat body, which is the primary site of synthesis for the large extratesticular pool, cells of the testes sheath secrete glycosylated storage proteins assembled into hexamers. The testis sheath differed from fat body in several important respects, including the failure to synthesize an abundant (in the hemolymph) 74,000-Mr storage protein, its relatively reduced expression of the 76,000-Mr polypeptide, and the absence of resorption of storage proteins from the lumen of the testis during pupal development. Cyst cells were also shown to import actively the 82,000-Mr storage protein by pinocytosis of testicular fluid and transfer it to the developing spermatids. Unlike other cell types that sequester storage proteins in the form of cytoplasmic granules, their localization within spermatids was exclusively mitochondrial. These observations suggest that expression of the storage protein genes is regulated tissue specifically and reveal novel pathways for their transport and, perhaps, utilization and function during development.
    Additional Material: 10 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 29 (1995), S. 381-390 
    ISSN: 0739-4462
    Keywords: cell line ; development ; Manduca sexta ; apolipoprotein III ; polypeptide ; vesicles ; Trichoplusia ni ; wing discs ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: An N-terminal amino acid sequence of a 16.9 kDa hemolymph polypeptide, “Vesicle Promoting Factor” (VPF) from Trichoplusia ni, revealed a high sequence homology (70%) with Manduca sexta apolipophorin-III. A polyclonal antibody developed against VPF, however, was not immunoreactive with either purified M. sexta or T. ni apolipophorin-III. Immunoblots of tissue homogenates of T. ni indicated that VPF was present in imaginal wing discs, central nervous system (CNS), silk glands, midgut and hemocytes from fifth instar larvae, and also in the IAL-TND1 cell line which can grow as either fluid-filled multicellular vesicles or multicellular aggregates. VPF was also detected immunologically in the hemolymph of adults of T. ni, and in hemolymph of adults and larvae of Galleria mellonella and Heliothis virescens. Testes, midgut, hemocytes, and wing discs, but not Malpighian tubules, of T. ni released VPF into tissue culture medium during a 3 h incubation period. © 1995 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
    Additional Material: 5 Ill.
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