Kuo W N
Mol Cell Biochem. 1984 Sep;64(1):39-44. doi: 10.1007/BF00420926.
Multiforms of megamodulin-dependent protein kinases (M-PK) were partially purified from baker's yeast by excluding endogenous megamodulin with histone, and then by gel filtration with Sephadex G-200. The stimulation of M-PK in the presence of Mg2+, Mn2+ or Co2+ was enhanced by yeast megamodulin. In addition, similar augmented activity of M-PK was also noted in the presence of Mg2+ by megamodulins prepared from E. coli, bovine brain and wheat germ.
通过用组蛋白去除内源性巨调节蛋白,然后用葡聚糖凝胶G-200进行凝胶过滤,从面包酵母中部分纯化了多形式的巨调节蛋白依赖性蛋白激酶(M-PK)。酵母巨调节蛋白增强了在Mg2+、Mn2+或Co2+存在下M-PK的活性。此外,由大肠杆菌、牛脑和小麦胚芽制备的巨调节蛋白在Mg2+存在下也观察到了M-PK类似的增强活性。