Randall C C, Rogers H W, Downer D N, Gentry G A
J Virol. 1972 Feb;9(2):216-22. doi: 10.1128/JVI.9.2.216-222.1972.
A protein kinase which is intimately associated with equine herpesvirus (equine abortion virus) was found by using adenosine triphosphate-gamma-(32)P as a phosphate donor and virus protein as an acceptor. Consistent demonstration of the activity requires prior removal of phosphohydrolase. The kinase activity requires Mg(2+), is not stimulated by cyclic adenosine monophosphate, but is enhanced by added protamine or arginine-rich histone. The labeled product is resistant to ribonuclease, deoxyribonuclease, and chloroform-methanol but is sensitive to Pronase. Other tests suggest that serine and threonine residues are the acceptor sites. In the in vitro reaction, the incorporation represents an average of approximately 4,500 phosphate residues per virion, and all 17 virus protein bands resolved by polyacrylamide gel electrophoresis appear to be labeled.
通过使用三磷酸腺苷-γ-(32)P作为磷酸供体，病毒蛋白作为受体，发现了一种与马疱疹病毒（马流产病毒）密切相关的蛋白激酶。该活性的持续证明需要事先去除磷酸水解酶。激酶活性需要Mg(2+)，不受环磷酸腺苷刺激，但添加鱼精蛋白或富含精氨酸的组蛋白可增强其活性。标记产物对核糖核酸酶、脱氧核糖核酸酶和氯仿-甲醇具有抗性，但对链霉蛋白酶敏感。其他测试表明丝氨酸和苏氨酸残基是受体位点。在体外反应中，每个病毒粒子的掺入平均代表约4500个磷酸残基，并且通过聚丙烯酰胺凝胶电泳分离的所有17条病毒蛋白带似乎都被标记。
