Document Detail

Identity and substrate specificity of human erythrocyte membrane-bound and cytosolic casein kinases.
MedLine Citation:
PMID:  1959595     Owner:  NLM     Status:  MEDLINE    
The relationship and substrate specificity of the human erythrocyte membrane kinase and casein kinase A were investigated. Based on Staphylococcus aureus V8 protease digestion patterns, the 2 kinases appeared to be structurally homologous. These enzymes also exhibited the same substrate specificity and phosphorylated the same synthetic peptides and domains of ankyrin. Both kinases did not utilize GTP effectively as a substrate and were not inhibited by low concentrations of heparin, suggesting that they were type I casein kinases. An analysis of synthetic peptide phosphorylation failed to reveal a specific pattern of recognition of the amino acid sequence surrounding the phosphorylation site.
T Wei; M Tao
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  FEBS letters     Volume:  292     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1991 Nov 
Date Detail:
Created Date:  1992-01-07     Completed Date:  1992-01-07     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  141-4     Citation Subset:  IM    
Department of Biochemistry, University of Illinois, Chicago 60612.
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MeSH Terms
Amino Acid Sequence
Casein Kinases
Cytosol / enzymology*
Electrophoresis, Polyacrylamide Gel
Erythrocyte Membrane / enzymology*
Molecular Sequence Data
Peptide Mapping
Protein Kinases / metabolism*
Substrate Specificity
Grant Support
Reg. No./Substance:
EC 2.7.-/Protein Kinases; EC Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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