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Phosphorylation of lysine rich histones using histone kinase from pig brain


, : Phosphorylation of lysine rich histones using histone kinase from pig brain. Molekulyarnaya Biologiya (Moscow) 10(2): 360-366

The phosphorylation of lysine-rich histones F1, F2a2 and F2b of calf thymus was investigated using homogeneous histone kinase from pig brain. 32P-labeled 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.

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