[猪脑组蛋白激酶对富含赖氨酸组蛋白的磷酸化作用]
[Phosphorylation of lysine-rich histones by swine brain histokinase].
作者信息
Shliapnikov S V, Arutiunian A A, Kurochkin S N, Memelova L V, Nesterova M V
出版信息
Mol Biol (Mosk). 1976 Mar-Apr;10(2):360-6.
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.
利用来自猪脑的均一化组蛋白激酶，对小牛胸腺富含赖氨酸的组蛋白F1、F2a2和F2b的磷酸化作用进行了研究。获得了相应组蛋白胰蛋白酶消化产物的32P标记磷酸肽。根据N端分析以及所获得放射性肽的氨基酸组成定量测定结果，在富含赖氨酸组蛋白的一级结构中确定了磷酸化位点，即组蛋白F1多肽链的Ser-38、组蛋白F2a2的Ser-19或18以及组蛋白F2b的Ser-14和36。因此，证明了脑组蛋白激酶在体外具有高度特异性。
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