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  • Title: Protein kinases in rat testes: evidence for different fractions of the enzyme.
    Author: Bernard EA, Wassermann GF.
    Journal: Can J Biochem; 1975 Feb; 53(2):207-14. PubMed ID: 236080.
    Abstract:
    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.
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