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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
1983-8-17
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pubmed:abstractText |
C-proteins have been isolated from rabbit red skeletal muscle (soleus and semitendinosus) and cardiac muscle and their structure and properties compared with those of white muscle C-protein. The Mr of white, red, and cardiac C-proteins are 135,000, 145,000, and 150,000, respectively, and their s20,w values are 4.3, 3.8, and 4.8 S, indicating that red C-protein is more asymmetric than the other two. They elute quite differently from hydroxylapatite columns. Two-dimensional CNBr peptide maps show extensive differences in primary structure, and anti-white C-protein does not precipitate red or cardiac C-protein. Despite these structural differences, all three C-proteins bind equally to white, red, or cardiac myosin and to actin. All three have the same effects on actomyosin ATPase in 50 mM KCl; they inhibit red and white skeletal actomyosins but slightly activate cardiac actomyosin. X-protein, a 140,000-dalton contaminant of white C-protein, was also investigated. It is very similar to red C-protein in elution from hydroxylapatite columns, S20,w, amino acid composition, and primary structure, but small differences in Mr and peptide maps indicate that the two proteins are probably not identical.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/citrate-binding transport protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8395-401
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6134729-Amino Acids,
pubmed-meshheading:6134729-Animals,
pubmed-meshheading:6134729-Carrier Proteins,
pubmed-meshheading:6134729-Kinetics,
pubmed-meshheading:6134729-Molecular Weight,
pubmed-meshheading:6134729-Muscle, Smooth,
pubmed-meshheading:6134729-Muscles,
pubmed-meshheading:6134729-Myocardium,
pubmed-meshheading:6134729-Myosins,
pubmed-meshheading:6134729-Organ Specificity,
pubmed-meshheading:6134729-Peptide Fragments,
pubmed-meshheading:6134729-Protein Binding,
pubmed-meshheading:6134729-Rabbits
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pubmed:year |
1983
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pubmed:articleTitle |
The C-proteins of rabbit red, white, and cardiac muscles.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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