| pubmed-article:6214253 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C0027108 | lld:lifeskim |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C0205470 | lld:lifeskim |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C1882417 | lld:lifeskim |
| pubmed-article:6214253 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6214253 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6214253 | pubmed:dateCreated | 1982-10-29 | lld:pubmed |
| pubmed-article:6214253 | pubmed:abstractText | Antibodies specific for rabbit fast-twitch-muscle myosin LCIF light chain were purified by affinity chromatography and characterized by both non-competitive and competitive enzyme-linked immunosorbent assay (ELISA) and a gel-electrophoresis-derived assay (GEDELISA). The antibodies did not cross-react with myosin heavy chains, and were weakly cross-reactive with the LC2F [5,5'-dithio-(2-nitrobenzoic acid)-dissociated] light chain and with all classes of dissociated light chains (LC1Sa, LC1Sb and LC2S), as well as with the whole myosin, from hind-limb slow-twitch muscle. The immunoreactivity of myosins with a truly mixed light-chain pattern (e.g. vastus lateralis and gastrocnemius) correlated with percentage content of fast-twitch-muscle-type light chains. A more extensive immunoreactivity was observed with diaphragm and masseter myosins, which were also characterized, respectively, by a relative or absolute deficiency of LC1Sa light chain. Furthermore, it was found that the LC1Sb light chain of masseter myosin is antigenically different from its slow-twitch-muscle myosin analogue, and is immunologically related to the LC1F light chain. Rabbit masseter muscle from its metabolic and physiological properties and the content, activity and immunological properties of sarcoplasmic-reticulum adenosine triphosphatase, is classified as a red, predominantly fast-twitch, muscle. Therefore our results suggest that the two antigenically different iso-forms of LC1Sb light chain are associated with the myosins of fast-twitch red and slow-twitch red fibres respectively. | lld:pubmed |
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| pubmed-article:6214253 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6214253 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6214253 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6214253 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6214253 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:6214253 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6214253 | pubmed:author | pubmed-author:MargrethAA | lld:pubmed |
| pubmed-article:6214253 | pubmed:author | pubmed-author:SalviatiGG | lld:pubmed |
| pubmed-article:6214253 | pubmed:author | pubmed-author:BiralDD | lld:pubmed |
| pubmed-article:6214253 | pubmed:author | pubmed-author:VolpePP | lld:pubmed |
| pubmed-article:6214253 | pubmed:author | pubmed-author:DamianiEE | lld:pubmed |
| pubmed-article:6214253 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6214253 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6214253 | pubmed:volume | 203 | lld:pubmed |
| pubmed-article:6214253 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6214253 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6214253 | pubmed:pagination | 529-40 | lld:pubmed |
| pubmed-article:6214253 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:6214253 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6214253 | pubmed:articleTitle | Polymorphism of myosin light chains. An electrophoretic and immunological study of rabbit skeletal-muscle myosins. | lld:pubmed |
| pubmed-article:6214253 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6214253 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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