Kochetkov S N, Gabibov A G, Mar'iash L I, Shibnev V A, Severin E S
Mol Biol (Mosk). 1984 Jul-Aug;18(4):901-6.
A study was made of the specificity of the catalytic subunit of cAMP-dependent pig brain protein kinase with respect to structural analogs of the protein substrate, histone H1, namely: a) high-molecular-weight histone fragments obtained as the result of specific cleavage of histone with trypsin and N-bromsuccinimide; b) synthetic peptides-substrates; c) synthetic peptides-inhibitors. Analysis of the kinetic parameters estimated for these compounds allowed to evaluate the individual contribution of various elements of the primary and three-dimensional structure of histone in the processes of binding and phosphorylation. Factors of "near" and "remote" specificity in the protein substrate binding are suggested.
对猪脑cAMP依赖性蛋白激酶催化亚基相对于蛋白质底物组蛋白H1的结构类似物的特异性进行了研究，这些类似物包括：a）通过用胰蛋白酶和N-溴代琥珀酰亚胺对组蛋白进行特异性切割得到的高分子量组蛋白片段；b）合成肽底物；c）合成肽抑制剂。对这些化合物估计的动力学参数进行分析，有助于评估组蛋白一级和三维结构的各个元素在结合和磷酸化过程中的个体贡献。提出了蛋白质底物结合中“近”和“远”特异性的因素。
