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PMID: 2983313 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A synthetic peptide substrate specific for casein kinase II.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 3 ·1985-02-00 ·Pages 737-41

Kuenzel EA, Krebs EG

Abstract

A synthetic peptide having the sequence Arg-Arg-Arg-Glu-Glu-Thr-Glu-Glu-Glu was found to serve as a convenient substrate for the protein kinase generally referred to as casein kinase II. The enzyme exhibited an apparent Km of 500 microM for the peptide, as compared to an apparent Km of 50 microM for casein. The maximum velocities for phosphorylation of the peptide and of casein were similar. The peptide was not phosphorylated by any of eight other protein kinases, all of which were shown to be active toward their known substrates. The peptide was used to monitor activity during steps in the purification of casein kinase II from bovine liver. These experiments demonstrated that with this peptide it is now possible to obtain specific measurements of casein kinase II activity in crude enzyme preparations.

MeSH Terms
Animals Casein Kinases Cattle Cyclic AMP/metabolism Cyclic GMP/metabolism Epidermal Growth Factor/metabolism Heparin/pharmacology Humans Insulin/metabolism Kinetics Oligopeptides/chemical synthesis,metabolism Phosphorylation Protein Kinases/metabolism Rabbits Substrate Specificity
Chemicals
Insulin Oligopeptides Epidermal Growth Factor Heparin Cyclic AMP Protein Kinases Casein Kinases Cyclic GMP
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kuenzel E A
Krebs E G
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34 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.82.3.737
Published
1985-02-00
Pages
737-41
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397121
Subset
IM
Grants
NHLBI NIH HHS · HL-07312 · United States
External Links
PubMed source DOI: 10.1073/pnas.82.3.737 PMC Full Text View journal details
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