Document Detail


Purification and characterization of naturally occurring and in vitro induced multiple forms of MM creatine kinase.
MedLine Citation:
PMID:  6698986     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
MM creatine kinase purified from tissue exists as a single form but upon release into the plasma exhibits three forms which, based on increasing anodal migration on polyacrylamide gel electrophoresis, are referred to as MM1, MM2, and MM3. The three forms were isolated in pure form from plasma in sufficient quantities for biochemical and physiological studies. Chromatofocusing results show that MM1, MM2, and MM3 have distinct isoelectric points of 7.58, 7.43, and 7.30, respectively. Analysis on high pressure liquid chromatography showed MM1 and tissue creatine kinase (MMt) to have identical peptide maps, but MM2 and MM3 were different in at least one amino acid. Tissue MM creatine kinase was converted in vitro to MM2 and MM3 after incubation in plasma. Conversion was unaffected by nonspecific proteases but inhibited by benzoylarginine, epsilon-amino caproic acid, and guanidinoethylmercaptosuccinic acid, specific inhibitors of carboxypeptidase N. Digestion of purified tissue MM creatine kinase with carboxypeptidases N and B produced MM2 and MM3 which were identical with the forms produced in vivo. Hybridization experiments with MM1 plus MM3 produced all three forms, as did tissue MM creatine kinase plus MM2. MM2 was also able to produce all three forms in the experiments. The plasma half-life of tissue MM creatine kinase or MM1 was shown to be about one-half that of MM3. The results suggest that hydrolytic cleavage of a basic amino acid, presumably by carboxypeptidase N, is responsible for conversion of MMt to MM2 and MM3. COOH-terminal amino acid analysis demonstrated the COOH-terminal amino acid of canine and rabbit MM1 to be lysine. Thus, we conclude that cleavage of the COOH-terminal lysine from MMt by serum carboxypeptidase N generates two additional MM creatine kinase isoforms with prolonged plasma clearance rates.
Authors:
S George; Y Ishikawa; M B Perryman; R Roberts
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  259     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1984 Feb 
Date Detail:
Created Date:  1984-04-10     Completed Date:  1984-04-10     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2667-74     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Carboxypeptidases
Creatine Kinase / blood*,  isolation & purification
Dogs
Electrophoresis, Polyacrylamide Gel
Half-Life
Isoelectric Focusing
Isoenzymes
Kinetics
Myocardial Infarction / enzymology
Rabbits
Grant Support
ID/Acronym/Agency:
HL 17646/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Isoenzymes; EC 2.7.3.2/Creatine Kinase; EC 3.4.-/Carboxypeptidases

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