[Skeletal muscle troponin and phosphorylation: a site of troponin T, that is phosphorylated by specific protein kinase].
A procedure is described of the isolation of protein kinase, which phosphorylates isolated troponin T with a rate, 5--30 fold exceeding the phosphorylation rate of other substrates (phosvitine, caseine, protamine sulphate, H1, H2A, H2b, H3, H4 histones). Troponin T-specific protein kinase transfers 0.85--0.95 moles of P per 1 mol of dephosphorylated troponin T. It phosphorylates only N-terminal acetylated serine residue, i. e. the site of troponin T structure, which is normally phosphorylated, when the whole troponin complex is isolated from skeletal muscles. Protein kinase is incapable to phosphorylate N-terminal serine residue in a mixture of triptic peptides of troponon T.
D000818:Animals; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D010750:Phosphoproteins / Q000096:biosynthesis; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D012694:Serine / Q000378:metabolism; D014336:Troponin / Q000378:metabolism*
D009124:Muscle Proteins; D010750:Phosphoproteins; D014336:Troponin; D012694:Serine; D011494:Protein Kinases
Tropenin skeletnykh myshts i fosforilir vanie: uchastok troponina T, fosforiliruemyi spetisficheskoi proteinkinazoĭ.