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Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases

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Walsh, Donal A., Ashby, Charles D., Gonzalez, Carmen, Calkins, Dianne, Fischer, Edmond H., Krebs, Edwin G.·1971·Journal of Biological Chemistry

Abstract

The partial purification and characterization of a factor from skeletal muscle which inhibits the activity of adenosine 3',5'-monophosphate-dependent protein kinases from skeletal muscle, heart, liver, adipose tissue, and brain is described. The inhibitor is stable to heating at 96° and to precipitation with 5%, w/v, of trichloracetic acid, but is assumed to be a protein since it is inactivated by proteolytic enzymes. It has a molecular weight of 26,000 by gel exclusion and an S20,w of 1.5 by sucrose density gradient centrifugation. A kinetic analysis of the effect of the inhibitor on the phosphorylation of casein by skeletal muscle protein kinase indicates that it interacts noncompetitively with respect to ATP, the protein substrate, and adenosine 3',5'-monophosphate. The inhibitor promotes a 5-fold increase in the binding constant of adenosine 3',5'-monophosphate to the protein kinase.

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Metadata

Authors
Walsh, D. A., Ashby, C. D., Gonzalez, C., Calkins, D., Fischer, E. H., & Krebs, E. G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1971-04
Volume
246
Issue
7
Pages
1977-1985
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2141449078
Cited by
887
References
0
FWCI
13.94
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases. https://app.cochat.ai/papers/10.1016/s0021-9258(19)77177-4
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Walsh, D. A., Ashby, C. D., Gonzalez, C., Calkins, D., Fischer, E. H., & Krebs, E. G. (1971). Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)77177-4

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