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Changes in protein phosphorylation during the maturation of mammalian oocytes in vitro

✍ Scribed by Crosby, Ian M. ;Osborn, Jeremy C. ;Moor, Robert M.

Publisher: John Wiley and Sons
Year: 1984
Tongue: English
Weight: 829 KB
Volume: 229
Category: Article
ISSN: 0022-104X
DOI: 10.1002/jez.1402290313

No coin nor oath required. For personal study only.

✦ Synopsis

Cumulus-enclosed sheep oocytes were cultured in gonadotrophin-containing medium for up to 9 hr and were then incubated for 3 hr in the presence of [32P]phosphate. The incorporation of 32P into TCA-insoluble material was measured, and oocyte proteins were separated by one-and twodimensional gel electrophoresis.

Incorporation of [32P]phosphate into protein increased after 3 hr of culture and again after 9 hr, the time of germinal vesicle breakdown (GVBD). Qualitative and quantitative changes in the phosphorylation of proteins occurred over the 12-hr period studied. One of the most prominent changes was the appearance of a band of Mr 33,000, which was absent at 0-3 hr but appeared with increasing intensity with longer periods of culture. Two-dimensional electrophoresis revealed that the bulk of material in this band was a neutral polypeptide. No significant incorporation of [32P]phosphate was found in ribosomal extracts of oocytes.

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