[Phosphorylation of lysine-rich histones by swine brain histokinase].
The phosphorylation of lysine-rich histones F1, F2a2 and F2b of calf thymus has been investigated using homogeneous histone kinase from pig brain. 32P-labelled phosphopeptides from tryptic digests of corresponding histones were obtained. According to N-terminal analysis and the quantitative determination of amino acid composition of the obtained radioactive peptides the sites of phosphorylation were identified in the primary structure of lysine-rich histones, namely, Ser-38 for the polypeptide chain of histone F1, Ser-19 or 18 for histone F2a2 and Ser-14 and 36 for histone F2b. Thus, the high specificity of brain histone kinase in vitro was demonstrated.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D006657:Histones; D007700:Kinetics; D008239:Lysine; D008968:Molecular Conformation; D006656:Protamine Kinase; D011494:Protein Kinases; D013552:Swine
D006657:Histones; D011494:Protein Kinases; D006656:Protamine Kinase; D008239:Lysine
Fosforilirovanie bogatykh lizinom gistonov gistokinazoĭ iz mozga svin'i