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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1988-6-29
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pubmed:abstractText |
Substructure of chicken gizzard smooth muscle alpha-actinin molecule was deduced by domainal mapping of the proteolytic fragments with alpha-chymotrypsin. There were three chymotryptic cleavage sites (Sites I, II, and III, from the amino terminus). Cleavage at Site I generated two fragments, i.e. an NH2-terminal 36-kDa fragment and a COOH-terminal 70-kDa fragment. The 70-kDa fragment generated either a 55-kDa fragment by cleavage at Site II or a 65-kDa fragment by cleavage at Site III. Purified NH2-terminal 36-kDa fragment bound to F-actin, whereas the 55-kDa fragment formed a dimeric molecule. Circular dichroism and electron microscopic experiments demonstrated that the alpha-helical content of the 55-kDa fragment was 14% higher than that of native gizzard alpha-actinin, coinciding with the apparently rod-shaped configuration of this fragment. A 110-kDa product was generated from two 55-kDa fragments in a cross-linking study with the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. Two cross-linkable sites in the 55-kDa, A- and B-site, were shown to be involved in this reaction. Further, it was demonstrated by using N-(7-dimethylamino-4-methyl-3-coumarinyl)maleimide labeling and immunoblotting analyses that the A-site on one 55-kDa fragment was cross-linked to the B-site on the other. These results suggest that smooth muscle alpha-actinin formed an antiparallel dimeric molecule in which the 55-kDa fragments connected the two actin-binding domains composed of the 36-kDa fragments.
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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 |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7800-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3286641-Actinin,
pubmed-meshheading:3286641-Amino Acid Sequence,
pubmed-meshheading:3286641-Animals,
pubmed-meshheading:3286641-Chickens,
pubmed-meshheading:3286641-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3286641-Fluorescamine,
pubmed-meshheading:3286641-Immunosorbent Techniques,
pubmed-meshheading:3286641-Microscopy, Electron,
pubmed-meshheading:3286641-Molecular Weight,
pubmed-meshheading:3286641-Muscle, Smooth,
pubmed-meshheading:3286641-Peptide Mapping
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pubmed:year |
1988
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pubmed:articleTitle |
Substructure and higher structure of chicken smooth muscle alpha-actinin molecule.
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pubmed:affiliation |
Institute of Basic Medical Sciences, University of Tsukuba, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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