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- W1984095317 abstract "Cytoplasmic poly(A)+-RNA, prepared from fat bodies of reproductively active locust females, directed the synthesis of two large polypeptides in Xenopus oocytes. Occasionally two smaller polypeptides (X1 and X2) were also detectable. The two larger polypeptides were immunologically and electrophoretically indistinguishable from the unprocessed Vitellogenin polypeptides (Vg1 and Vg2) of locust fat bodies. Peptide patterns generated from these two translation products by Staphylococcus aureus V8 protease digestion were identical to those of Vg1 and Vg2. RNA isolated from allatectomized female locusts treated with the juvenile hormone analog (ZR-515) was also able to direct the synthesis of vitellogenin in Xenopus oocytes, whereas RNA isolated from mature males or allatectomized females did not. The molecular weights of fat-body Vg1 and Vg2 were 235,000 and 225,000, respectively and the processed vitellogenin polypeptides were found to range from 126,000 to 52,000. Electrophoretic and Chromatographic analysis of [35S]methionine-containing tryptic peptides of Vg1 and Vg2 showed two different tryptic peptide fingerprints. Distinctly different peptide patterns were also observed when Vg1 and Vg2 were partially digested with V8 protease or papain. However, tryptic peptide mapping and V8 protease limited digestion mapping of fat-body X1 and X2 revealed that these two polypeptides were derived from Vg1 and Vg2. This suggests that Vg1 and Vg2 are products of two different vitellogenin structural genes." @default.
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- W1984095317 date "1980-04-01" @default.
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- W1984095317 title "Vitellogenin in locusts (Locusta migratoria): Translation of vitellogenin mRNA in Xenopus oocytes and analysis of the polypeptide products" @default.
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- W1984095317 doi "https://doi.org/10.1016/0003-9861(80)90511-1" @default.
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