| pubmed-article:3286641 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3286641 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:3286641 | lifeskim:mentions | umls-concept:C1267092 | lld:lifeskim |
| pubmed-article:3286641 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:3286641 | lifeskim:mentions | umls-concept:C0917705 | lld:lifeskim |
| pubmed-article:3286641 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3286641 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:3286641 | pubmed:dateCreated | 1988-6-29 | lld:pubmed |
| pubmed-article:3286641 | 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. | lld:pubmed |
| pubmed-article:3286641 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3286641 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3286641 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3286641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3286641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3286641 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3286641 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3286641 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3286641 | pubmed:author | pubmed-author:EndoTT | lld:pubmed |
| pubmed-article:3286641 | pubmed:author | pubmed-author:KurodaMM | lld:pubmed |
| pubmed-article:3286641 | pubmed:author | pubmed-author:TanakaTT | lld:pubmed |
| pubmed-article:3286641 | pubmed:author | pubmed-author:ImamuraMM | lld:pubmed |
| pubmed-article:3286641 | pubmed:author | pubmed-author:MasalaCC | lld:pubmed |
| pubmed-article:3286641 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3286641 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3286641 | pubmed:volume | 263 | lld:pubmed |
| pubmed-article:3286641 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3286641 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3286641 | pubmed:pagination | 7800-5 | lld:pubmed |
| pubmed-article:3286641 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:meshHeading | pubmed-meshheading:3286641-... | lld:pubmed |
| pubmed-article:3286641 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3286641 | pubmed:articleTitle | Substructure and higher structure of chicken smooth muscle alpha-actinin molecule. | lld:pubmed |
| pubmed-article:3286641 | pubmed:affiliation | Institute of Basic Medical Sciences, University of Tsukuba, Japan. | lld:pubmed |
| pubmed-article:3286641 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3286641 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3286641 | lld:pubmed |
