Purification of phosphoprotein phosphatase from bovine cardiac muscle that catalyzes dephosphorylation of cyclic AMP-binding protein component of protein kinase.-Reference-Cited by-同舟云学术

Purification of phosphoprotein phosphatase from bovine cardiac muscle that catalyzes dephosphorylation of cyclic AMP-binding protein component of protein kinase.

Published:1977-05 Issue:9 Volume:252 Page:2855-2859
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chou C K,Alfano J,Rosen O M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Purification and properties of rabbit liver phosphorylase phosphatase.

2. CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASES, IV. WIDESPREAD OCCURRENCE OF ADENOSINE 3',5'-MONOPHOSPHATE-DEPENDENT PROTEIN KINASE IN VARIOUS TISSUES AND PHYLA OF THE ANIMAL KINGDOM

3. Regulation of Adenosine 3′,5′-Monophosphate-dependent Protein Kinase

4. A cyclic-3′,5′-adenosine monophosphate dependent protein kinase from the adrenal cortex: Comparison with a cyclic AMP binding protein

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