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  • Articles  (4)
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (4)
  • Wiley-Blackwell  (4)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991), S. 143-155 
    ISSN: 0739-4462
    Keywords: reproduction ; vitellin ; Hymenoptera ; caste ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Vitellogenin has been identified in the ant Camponotus festinatus, both in queens and workers. In the workers, it is already present before adult eclosion in low concentrations (〈1 μg/μl hemolymph). Vitellogenin and vitellin are immunologically identical and are composed of a single type of apoprotein with an apparent Mr = 185,000. The molecular weight of the native molecules was estimated as ∼460,000 by pore limiting gradient electrophoresis. Vitellogenin was detected as a major protein in the hemolymph of young workers, both under queenright and queenless conditions. Thus, in spite of their sterility in the presence of the queen, C. festinatus workers are able to synthetize vitellogenin which is identical both in size and immunologically to the queen vitellogenin. About 6-7 weeks after adult eclosion, however, vitellogenin was usually undetectable in the hemolymph of queenright workers, particularly the minor workers, while it constituted about 30% of total protein in queenless workers. Protein concentration in the hemolymph of queenless insects increased up to 20-fold as compared to 1-day-old insects. Queenless workers also developed large amounts of perivisceral fat body, while queenright workers, particularly the minor workers, showed a dramatic fat body regression about 6 weeks after emergence.
    Additional Material: 7 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 211-220 
    ISSN: 0739-4462
    Keywords: pheromone biosynthesis-activating neuropeptide ; calling behavior ; Lepidoptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Adult females of Spodoptera littoralis (Lepidoptera: Noctuidae) showed a cyclic pattern of sex pheromone production, and high titers of (Z,E)-9,11-tetradecadienyl acetate, the major component of its pheromone blend, were only detected during scotophase. Maximal amounts of pheromone were extracted approximately 2 h into second scotophase. Decapitation before the beginning of darkness inhibited normal production of pheromone, and no calling behavior was observed. Injection of brain-suboesophageal ganglion (Br-SOG) homogenate at the onset of scotophase restored pheromone production in decapitated females to the levels characteristic of second scotophase. Pheromone biosynthesis was also stimulated in decapitated females during photophase. The response to Br-SOG homogenate injection was dose-dependent. The pheromonotropic activity of Br-SOG extract was the same when females were injected during photophase or scotophase.
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  • 3
    ISSN: 0739-4462
    Keywords: Bacillus thuringiensis ; Phthorimaea operculella ; insecticidal crystal protein ; receptors ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The potato tuber moth is susceptible to at least three insecticidal crystal proteins (ICPs) from Bacillus thuringiensis: CrylA(b), CrylB, and CrylC. To design useful combinations of toxin genes either in transgenic plants or in new genetically modified B. thuringiensis strains, it is necessary to determine the binding characteristics of the different ICPs so as not to combine a pair sharing the same binding site. This has been accomplished using two different techniques: 125I-labeling of the ICPs with further measurement of the radioactivity bound to brush border membrane vesicles, and microscopic visualization of the bound ICPs by enzyme-linked reagents such as antibodies or streptavidin using biotinylated ICPs. Our results show that CrylA(b), CrylB, and CrylC bind to different sites in the brush border membrane of midgut epithelial cells. Also, the affinity of the binding sites for the ICPs and their concentration in brush border membrane vesicles has been determined in a laboratory strain and a storage collected population. No significant differences were found between these two strains. © 1994 Wiley-Liss, Inc.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 6 (1987), S. 49-58 
    ISSN: 0739-4462
    Keywords: juvenile hormone ; vitellogenic oocytes ; yolk proteins ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Using polyacrylamide gel electrophoresis (PAGE) under denaturing conditions, two major polypeptides of 200,000 and 170,000 daltons were detected in the hemolymph of mature female Oncopeltus fasciatus, but they were not found in the hemolymph of males or newly emerged females. Those polypeptides constituted the two major bands of early vitellogenic oocytes; however, they were absent from the yolk of mature eggs. The slower-migrating band (200,000 daltons) appears to correspond to a vitellogenic protein already identified in O. fasciatus, whose synthesis has been suggested to be independent of juvenile hormone (JH). Treatment of newly emerged adult females with the corpus allatum cytotoxin precocene II prevented the appearance of the female-specific bands and induced an important accumulation of other proteins in the hemolymph. Yolk deposition was also inhibited in those animals. Topical application of JH to precocene-treated females restored the appearance of the 200,000 and 170,000 dalton polypeptides in the hemolymph. These results suggest that JH is required for the synthesis of female-specific polypeptides in O. fasciatus.
    Additional Material: 5 Ill.
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