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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1992-12-7
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pubmed:abstractText |
The amino-acid sequence of the short subfragment-2 in the amino-terminal portion of subfragment-2 derived from adult chicken ventricular muscle myosin was completely determined by direct protein analysis. Peptides fragmented by cyanogen bromide, lysyl endopeptidase and arginyl endopeptidase of S-carboxymethylated S-2 and peptides of large CNBr peptides cleaved by dilute formic acid were separated and sequenced. This short S-2 composed of 259 amino-acid residues was found highly conserved and contained hydrophobic and charged residue repeat units. Comparing this sequence with the partial nucleotide sequence of cDNA corresponding to short S-2 (Stewart A.F.R., et al. (1991) J. Mol. Evol. 33, 357-366), a 64 amino-acid residues extension towards the NH2 terminus and 9 residues differences were observed. Furthermore, this sequence is compared with those of rat, rabbit and human ventricular myosins, and 86.1%, 86.5%, 86.5% sequence identities are observed, respectively.
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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 |
Oct
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pubmed:issn |
0177-3593
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
373
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1045-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1418675-Amino Acid Sequence,
pubmed-meshheading:1418675-Animals,
pubmed-meshheading:1418675-Chickens,
pubmed-meshheading:1418675-Molecular Sequence Data,
pubmed-meshheading:1418675-Myocardium,
pubmed-meshheading:1418675-Myosins,
pubmed-meshheading:1418675-Sequence Analysis,
pubmed-meshheading:1418675-Sequence Homology, Amino Acid,
pubmed-meshheading:1418675-Serine Endopeptidases
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pubmed:year |
1992
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pubmed:articleTitle |
Amino-acid sequence of the short subfragment-2 in adult chicken cardiac muscle myosin.
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pubmed:affiliation |
School of Allied Medical Sciences, Nagasaki University, Japan.
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pubmed:publicationType |
Journal Article
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