Document Detail


Comparison of substrate recognition by protein kinase C (type III) between rat liver cytosolic and particulate fractions.
MedLine Citation:
PMID:  2338165     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. Phosphorylation of rat liver endogenous substrates by protein kinase C (type III) was compared between cytosolic and particulate (mitochondria, microsomes and plasma membrane) fractions. 2. The rate and the maximum level of protein phosphorylation were several-fold higher in particulate fractions than in cytosolic fraction. 3. Protein phosphorylation in cytosolic fraction was dependent on both Ca2+ and phospholipid, but only Ca2+ was necessary in phosphorylation of particulate fractions. 4. These results suggest that protein kinase C (type III) has much more target proteins in particulate fractions rather than in cytosolic fraction and Ca2+ was important regulator in particulate protein phosphorylation.
Authors:
E Hashimoto; H Yamamura
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Publication Detail:
Type:  Comparative Study; In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The International journal of biochemistry     Volume:  22     ISSN:  0020-711X     ISO Abbreviation:  Int. J. Biochem.     Publication Date:  1990  
Date Detail:
Created Date:  1990-06-21     Completed Date:  1990-06-21     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0250365     Medline TA:  Int J Biochem     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  405-10     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Fukui Medical School, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / metabolism
Cytosol / metabolism
Liver / metabolism*
Microsomes, Liver / metabolism
Mitochondria, Liver / metabolism
Phosphorylation
Protein Kinase C / metabolism*
Proteins / metabolism
Rats
Rats, Inbred Strains
Subcellular Fractions / metabolism
Substrate Specificity
Chemical
Reg. No./Substance:
0/Proteins; EC 2.7.11.13/Protein Kinase C

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