Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological considerations.

摘要: Vitellogenin serves as the plasma precursor for yolk proteins, lipovitellin and phosvitin, in nonmammalian vertebrates. 32P-Vitellogenin was isolated from of teleost, Fundulus heteroclitus, used both to label phosvitin ovary indicate region preparative chromatographs ovarian extracts on DEAE-cellulose. Crude [32P]phosvitin could be resolved further into two labeled components with shallow gradients DEAE-cellulose eight by electrophoresis 12% polyacrylamide gels. Only largest electrophoretically correlated Coomassie Blue staining bands, but several smaller indicated cationic carbocyanine dye, Stains-all. Stains-all-dyed were also generally multiple bands. The a reproductively active female contains vitellogenic oocytes, postvitellogenic oocytes undergoing maturation prior ovulation, ovulated eggs. Examination various types follicles eggs gels revealed that during maturation, formed vitellogenesis either disappear or diminish, while appear. transformation can achieved vitro incubating prematurational saline medium containing deoxycorticosterone. These preliminary results demonstrate complex array phosvitin-like are present within single F. heteroclitus. We postulate one reason anomalous proteins found thus far teleost is some derived vitellogenin undergo proteolysis oocyte maturation.