[Protein phosphorylation in normal and neoplastic hepatocytes].
Partially purified preparations of protein kinase were isolated from the cytoplasm and nuclei of rat liver and hepatoma 27 and characterized in terms of their substrate specificity. The protein kinases from normal liver and hepatoma revealed some differences in phosphorylating protein substrates. Hepatoma protein kinases were found to phosphorylate arginine-rich histones (H3, H4); differences in phosphorylation of histone H1 were revealed. Hepatoma protein kinases phosphorylated the C-terminal fragment of histone H1, whereas normal liver protein kinases produced no such effect. It was assumed that the phosphorylation of histone H1 in rapidly dividing and resting cells is operated through different channels.
D000818:Animals; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D002467:Cell Nucleus / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008113:Liver Neoplasms / Q000201:enzymology*; D009374:Neoplasms, Experimental / Q000201:enzymology; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D011494:Protein Kinases; D006656:Protamine Kinase
Fosforilirovanie belkov v normal'nykh gepatotsitakh i PRI gepatome.