Kleiman J H, Moss B
J Biol Chem. 1975 Apr 10;250(7):2420-9.
A novel protein kinase that requires protamine as an activator to catalyze the phosphorylation of viral acceptor proteins was extracted from vaccinia virus cores with deoxycholate and purified 250-fold by DNA-cellulose and DEAE-cellulose column chromatography. The enzyme has a molecular weight of 62,000 as determined by sucrose gradient sedimentation. Two heat-stable phosphate acceptor proteins were extracted from virus particles with a nonionic detergent and purified by heat treatment, precipitation with organic solvents, and CM-cellulose chromatography. The molecular weights of the phosphate acceptor proteins, determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, are 38,500 and 11,700.
一种新型蛋白激酶从痘苗病毒核心中用脱氧胆酸盐提取出来，该激酶需要鱼精蛋白作为激活剂来催化病毒受体蛋白的磷酸化，然后通过DNA纤维素和DEAE纤维素柱色谱法纯化了250倍。通过蔗糖梯度沉降法测定，该酶的分子量为62,000。用非离子去污剂从病毒颗粒中提取出两种热稳定的磷酸受体蛋白，并通过热处理、有机溶剂沉淀和CM纤维素色谱法进行纯化。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定，磷酸受体蛋白的分子量分别为38,500和11,700。
