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Comparison of the enzymatic activities of native and recombinant protein phosphatase-1 toward histone.

作者信息

Zhao S, Zhang Z, Lee Y C

机构信息

Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, FL 33101.

出版信息

Biochem Mol Biol Int. 1994 Nov;34(5):1027-33.

PMID:7703899
Abstract

The activities of native and recombinant rabbit muscle protein phosphatase-1 toward phosphorylated lysine-rich histone and phosphorylase a were compared. The activity of rabbit muscle protein phosphatase-1 toward histone is strongly stimulated by Mn++. In the case of the recombinant enzyme, both phosphorylase phosphatase and histone phosphatase activities exhibit a dependence on Mn++. Examination of the activities of both enzymes assayed under optimal conditions show that they exhibit similar substrate specificities toward histone and phosphorylase, contrary to previous claims (Alessi et al., Eur. J. Biochem. 213, 1055-1066, 1993).

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