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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1987-11-25
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pubmed:abstractText |
beta-Actinin is an actin-pointed end capping protein in skeletal muscle. Casella et al. have reported that a protein isolated from muscle acetone powder by procedures similar to those used for beta-actinin purification caps the barbed end of an actin filament (J. Biol. Chem. 261, 10915-10921 (1986)). We have confirmed the above results. However, it turned out that the two proteins were identical as to subunit sizes, peptide maps, and cross-reactivities with anti-beta-actinin IgG. The binding of the two proteins to opposite ends of an actin filament remains unexplained.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1481-3
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:3312183-Actin Depolymerizing Factors,
pubmed-meshheading:3312183-Actins,
pubmed-meshheading:3312183-Animals,
pubmed-meshheading:3312183-Chickens,
pubmed-meshheading:3312183-Destrin,
pubmed-meshheading:3312183-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3312183-Immunologic Techniques,
pubmed-meshheading:3312183-Isoelectric Focusing,
pubmed-meshheading:3312183-Microfilament Proteins,
pubmed-meshheading:3312183-Muscles
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pubmed:year |
1987
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pubmed:articleTitle |
Beta-actinin is not distinguishable from an actin barbed-end capping protein in chicken breast muscle.
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pubmed:affiliation |
Department of Biology, Faculty of Science, Chiba University.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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