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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (2)
  • Wiley-Blackwell  (2)
  • American Institute of Physics
  • National Academy of Sciences
  • 2020-2022
  • 1990-1994  (2)
Sammlung
Verlag/Herausgeber
  • Wiley-Blackwell  (2)
  • American Institute of Physics
  • National Academy of Sciences
Erscheinungszeitraum
Jahr
  • 1
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991), S. 143-155 
    ISSN: 0739-4462
    Schlagwort(e): reproduction ; vitellin ; Hymenoptera ; caste ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: 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.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 0739-4462
    Schlagwort(e): Bacillus thuringiensis ; Phthorimaea operculella ; insecticidal crystal protein ; receptors ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: 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.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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