Bernard E A, Wassermann G F
Can J Biochem. 1975 Feb;53(2):207-14. doi: 10.1139/o75-029.
Protein kinase activity of rat testis homogenate was separated into five fractions by means of pH 4.8 acidification and DEAE-cellulose chromatography. The five fractions showed a peculiar pattern of activity and cAMP dependency with the substrates used: casein, protamine, histone mixture, arginine-rich histone, lysine-rich histone, and phosvitin. The casein-sepharose substrate affinity column separated two fractions from the pH 4.8 precipitate. Peak number one phosphorylates histone preferently and is cAMP-dependent, while peak number tow has a strong affinity toward casein as substrate and is non cAMP-dependent.
通过pH 4.8酸化和DEAE-纤维素色谱法，将大鼠睾丸匀浆的蛋白激酶活性分离成五个组分。这五个组分在用酪蛋白、鱼精蛋白、组蛋白混合物、富含精氨酸的组蛋白、富含赖氨酸的组蛋白和卵黄高磷蛋白作为底物时，呈现出独特的活性模式和对环磷酸腺苷（cAMP）的依赖性。酪蛋白-琼脂糖底物亲和柱从pH 4.8沉淀中分离出两个组分。第一个峰优先磷酸化组蛋白且依赖cAMP，而第二个峰对酪蛋白作为底物具有很强的亲和力且不依赖cAMP。
