Characterization of protein kinases in mitotic and meiotic cell extracts.
A number of protein kinases have been separated and identified in extracts from mitotic and interphase culture cells and from mature and immature amphibian oocytes using nondenaturing polyacrylamide gel electrophoresis followed by in situ phosphorylation assays. Certain of these protein kinase activities appear to correlate with the biological activity of extracts, assayed by their ability to induce meiotic maturation following injection into Xenopus oocytes. These results are consistent with the notion that protein phosphorylation/dephosphorylation may be integral to the mechanisms of both nuclear membrane breakdown and chromosome condensation, events common and distinctive to mitosis and meiosis.
D000818:Animals; D005260:Female; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D008540:Meiosis; D008938:Mitosis; D009865:Oocytes / Q000201:enzymology; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D014982:Xenopus laevis
D011494:Protein Kinases; D006656:Protamine Kinase