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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 237-250 
    ISSN: 0739-4462
    Keywords: yolk phosphatase ; α-mannosidase ; Blattella germanica ; proteolytic processing ; vitellin ; embryo development ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Proteolytic processing of the vitellin in Blattella germanica eggs occurs 4 days postovulation and is correlated with both the onset of its utilization and the major portion of the embryo's growth. Yolk phosphatase is also expressed coincident with this event, and some aspects of its activation have been investigated. The enzyme is absent from the ooplasm (yolk) during the first 2 days following ovulation but increases approximately 20-fold in specific activity between days 3 and 4, when assayed at pH 3.9 or 4.8 and 9-fold at pH 6.5. No activation is observed for yolk-bound α-mannosidase, its specific activity remains elevated through the first 6 days following ovulation. This suggests that expression of the phosphatase is regulated independently of that of α-mannosidase in the yolk. Yolk with active phosphatase can dephosphorylate native vitellin, delipidated vitellin, and phosphocasein. Sucrose density gradient centrifugation of yolk obtained from eggs 4 days postovulation, revealed that phosphatase activity cosediments with material which reacts with antivitellin antibodies, while α-mannosidase and β-N-acetyl glucosaminidase are found near the top of the gradient. Oothecae derived from crossing certain translocational heterozygote males and wild-type females contain some eggs with severely depressed levels of yolk phosphatase in which embryos do not grow. Vitellin in these eggs fails to undergo proteolytic processing as late as day 5 postovulation and retains the subunit composition of freshly ovulated vitellin.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 13 (1990), S. 117-125 
    ISSN: 0739-4462
    Keywords: arylphorin ; Trichoplusia ni ; Chelonus ; parasitoid ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Arlyphorin (Ap) is the principal protein of the last larval instar hemolymph of Trichoplusia ni. It was shown to be homologous with the Aps of Manduca sexta and Lymantria dispar by Western blot and quantitative immunoelectrophoresis. Another hemolymph storage protein in T. ni of lesser titer was shown to be homologous with larval hemolymph protein (LSP) of M. sexta. Ap titer increased dramatically in the last larval instar of T. ni, as in other holometabolous insects studied. Parasitization by Chelonus sp. caused the Ap titer to rise prematurely in the penultimate larval instar of T. ni. This rise in Ap in the fourth instar is one of the earliest diagnostic signs of parasitization. Among the suite of behaviors of the Chelonus larva on exiting the host is depletion of the host cadaver of most remaining protein. The T. ni Ap titer in the alimentary tract of Chelonus peaks at that time and declines to zero in the first 24 h after parasitoid emergence, prior to its pupation. Aps are a source of phenolic storage compounds. Hence, premature induction of T. ni is advantageous for the parasitoid's own pupation and adult development.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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