Kuo W N
Biochem Biophys Res Commun. 1983 Jul 18;114(1):403-9. doi: 10.1016/0006-291x(83)91641-8.
Phosphoprotein phosphatases (PPase) were isolated from either the rabbit cerebral cortex or Baker's yeast by excluding endogenous megamodulin with histone, and then by desalting cations with Bio-Gel P-6DG filtration. The stimulation of PPase in the presence of Mn2+ was greatly enhanced by megamodulins prepared from various sources including rabbit brain, Baker's yeast, wheat germ, and Escherichia coli (E. coli). Moreover, the augmented activity of PPase was also demonstrated in the presence of [megamodulin-Mn2+] complex.
通过用组蛋白排除内源性巨调节蛋白,然后用Bio-Gel P-6DG过滤去除阳离子,从兔大脑皮层或面包酵母中分离出磷蛋白磷酸酶(PPase)。在存在Mn2+的情况下,PPase的活性受到来自各种来源(包括兔脑、面包酵母、小麦胚芽和大肠杆菌)制备的巨调节蛋白的极大增强。此外,在存在[巨调节蛋白-Mn2+]复合物的情况下,PPase的活性也得到了增强。