In:
Canadian Journal of Biochemistry, Canadian Science Publishing, Vol. 53, No. 2 ( 1975-02-01), p. 207-214
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 two has a strong affinity toward casein as substrate and is not cAMP-dependent.
Type of Medium:
Online Resource
ISSN:
0008-4018
Language:
English
Publisher:
Canadian Science Publishing
Publication Date:
1975
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