Nakaya N, Sugano N, Nishi A, Tsukada K
Biochim Biophys Acta. 1975 Dec 18;410(2):273-8. doi: 10.1016/0005-2744(75)90229-6.
A protein kinase (EC 2.7.1.37) which phosphorylates histones was purified partially from the soluble fractions of cultured plant cells. The optimum pH was 7.5 to 9.0. The activity wasnot stimulated by exogeneous cyclic AMP. It was thermolabile and completely dependent on the presence of Mg2+ or Mn2+ for activity. p-Chloromercuribenzoate inactivated this enzyme and this inactivation was overcome by mercaptoethanol.
一种能使组蛋白磷酸化的蛋白激酶(EC 2.7.1.37)从培养植物细胞的可溶性组分中得到了部分纯化。最适pH为7.5至9.0。外源环磷酸腺苷不会刺激其活性。它对热不稳定,活性完全依赖于Mg2+或Mn2+的存在。对氯汞苯甲酸可使该酶失活,而巯基乙醇可克服这种失活。