RNA-binding protein kinase from amphibian oocytes is a casein kinase II.
RNA-binding protein kinase from amphibian oocytes modifies serine and threonine residues in the molecules of substrates and utilizes both ATP and GTP. Low concentrations of heparin inhibit protein kinase. The foregoing suggests that this enzyme is casein kinase II. It is shown that RNA-binding proteins lack active forms of phosphatases and proteases which may affect the results of phosphorylation of both endogenous and exogenous substrates.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D047388:Casein Kinases; D004590:Electrophoresis, Paper; D005260:Female; D006160:Guanosine Triphosphate / Q000378:metabolism; D006493:Heparin / Q000494:pharmacology; D008970:Molecular Weight; D009865:Oocytes / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D011896:Rana temporaria
D012313:RNA; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D006493:Heparin; D011494:Protein Kinases; D047388:Casein Kinases