Document Detail

beta-actinin, a regulatory protein of muscle. Purification, characterization and function.
MedLine Citation:
PMID:  66229     Owner:  NLM     Status:  MEDLINE    
beta-Actinin, a minor regulatory protein of muscle, was purified from skeletal muscles of rabbit and chicken by DEAE-Sephadex chromatography. beta-Actinin consisted of two subunits, beta I and betaII, with chain weights of 37,000 and 34,000 daltons, respectively. The amino acid compositions were similar, though not identical. It appears that each of the two subunits is associated in solution. beta-Actinin had the following effects on actin: (1) inhibition of reassociation of F-actin fragments; (2) inhibition of network formation of F-actin; (3) inhibition of growth of F-actin fragments; (4) retardation of depolymerization of F-actin and (5) acceleration of polymerization of G-actin. All these actions of beta-actinin can be explained in terms of action as an "ending factor". Experimental evidence favored the view that beta-actinin is bound to one end of the F-actin filament, namely to the end opposite to the direction of polymerization. Fluorescence-labeled anti-beta-actinin stained the middle portion of the A band of myofibrils. Based on the finding that the stain was unchanged on removal of myosin, it is suggested that beta-actinin is located at the free ends of the I filaments of myofibrils. Thus is seems likely that beta-actinin functions as an ending factor for actin filaments.
K Maruyama; S Kimura; T Ishi; M Kuroda; K Ohashi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  81     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1977 Jan 
Date Detail:
Created Date:  1977-05-25     Completed Date:  1977-05-25     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  215-32     Citation Subset:  IM    
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MeSH Terms
Actinin / immunology,  isolation & purification,  metabolism*
Actins / metabolism
Adenosine Triphosphatases / metabolism
Amino Acids / analysis
Dactinomycin / metabolism
Macromolecular Substances
Microscopy, Electron
Molecular Weight
Muscle Proteins / metabolism*
Peptide Fragments / analysis
Reg. No./Substance:
0/Actins; 0/Amino Acids; 0/Macromolecular Substances; 0/Muscle Proteins; 0/Peptide Fragments; 11003-00-2/Actinin; 50-76-0/Dactinomycin; EC 3.6.1.-/Adenosine Triphosphatases

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