[Protein kinase, phosphatase and protease activities in a fraction of RNA-binding proteins].
The RNA-binding proteins from amphibian (Rana temporaria and Xenopus laevis) oocytes contain a cAMP-independent caseintype protein kinase activity. This enzyme can phosphorylate casein but does not phosphorylate histones. Using high voltage paper electrophoresis of acid hydrolysate of [32P]casein, it was found that P-O-phosphoserine and [32P]-O-phosphothreonine are formed via the phosphorylation reaction. Protein kinase retains the ability to bind poly(U) under physiological ionic strength values. It was shown that RNA-binding proteins do not contain any detectable forms of phosphatase or protease which might distort the results of phosphorylation of endogenous and exogenous substrates.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D005260:Female; D007700:Kinetics; D009865:Oocytes / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins; D011896:Rana temporaria; D013379:Substrate Specificity; D014981:Xenopus
D002352:Carrier Proteins; D016601:RNA-Binding Proteins; D012313:RNA; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D010447:Peptide Hydrolases
Issledovanie proteinkinaznoĭ, fosfataznoĭ i proteaznoĭ aktivnosteĭ vo fraktsii RNK-sviazyvaiushchikh belkov.