COMPARISON OF THE ENZYMATIC-ACTIVITIES OF NATIVE AND RECOMBINANT PROTEIN PHOSPHATASE-1 TOWARD HISTONE

Citation
Sm. Zhao et al., COMPARISON OF THE ENZYMATIC-ACTIVITIES OF NATIVE AND RECOMBINANT PROTEIN PHOSPHATASE-1 TOWARD HISTONE, Biochemistry and molecular biology international, 34(5), 1994, pp. 1027-1033
Citations number
21
Categorie Soggetti
Biology
ISSN journal
10399712
Volume
34
Issue
5
Year of publication
1994
Pages
1027 - 1033
Database
ISI
SICI code
1039-9712(1994)34:5<1027:COTEON>2.0.ZU;2-1
Abstract
The activities of native and recombinant rabbit muscle protein phospha tase-l toward phosphorylated lysine-rich histone and phosphorylase a w ere compared. The activity of rabbit muscle protein phosphatase-l towa rd histone is strongly stimulated by Mn++. In the case of the recombin ant enzyme, both phosphorylase phosphatase and histone phosphatase act ivities exhibit a dependence on Mn++ Examination of the activities of both enzymes assayed under optimal conditions show that they exhibit s imilar substrate specificities toward histone and phosphorylase, contr ary to previous claims (Alessi et al., fur. J. Biochem. 213, 1055-1066 , 1993).