Document Detail


Affinity chromatographic preparation of arterial heavy meromyosin subfragment-1.
MedLine Citation:
PMID:  134907     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Heavy meromyosin subfragment-1 (HMM S-1) was prepared by papain digestion of arterial myosin or actomyosin and was purified by agarose-ATP affinity chromatography. Proteolysis of crude arterial myosin suspensions was preceded by solubilization. HMM-S-1 thus obtained consisted mainly of a 90,000 dalton polypeptide and fully retained the K+- and Ca2+-ATPase of the parent myosin. Its affinity to agarose-ATP was comparable to that of skeletal muscle HMM S-1.
Authors:
R Lamed; U Mrwa
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Experientia     Volume:  32     ISSN:  0014-4754     ISO Abbreviation:  Experientia     Publication Date:  1976 Sep 
Date Detail:
Created Date:  1976-12-03     Completed Date:  1976-12-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376547     Medline TA:  Experientia     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  1221-2     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / isolation & purification
Animals
Calcium / pharmacology
Carotid Arteries / analysis*
Chromatography, Affinity
Molecular Weight
Myosin Subfragments / isolation & purification*
Papain
Peptide Fragments / isolation & purification
Potassium / pharmacology
Chemical
Reg. No./Substance:
0/Myosin Subfragments; 0/Peptide Fragments; 7440-09-7/Potassium; 7440-70-2/Calcium; EC 3.4.22.2/Papain; EC 3.6.1.-/Adenosine Triphosphatases

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


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