pubmed-article:1533157 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C0027108 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C1149668 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C1149245 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
pubmed-article:1533157 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
pubmed-article:1533157 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:1533157 | pubmed:dateCreated | 1992-5-28 | lld:pubmed |
pubmed-article:1533157 | pubmed:abstractText | The role of the N-terminal region of myosin light chain 1 (LC1) in actomyosin interaction was investigated using an IgG monoclonal antibody (2H2) directed against the N-terminal region of LC1. We defined the binding site of 2H2 by examining its cross-reactivity with myosin light chains from a variety of species and with synthetic oligopeptides. Our findings suggest that 2H2 is directed against the N-terminal region of LC1 which includes the trimethylated alanine residue at the N-terminus. In the presence of 2H2, the rate of actomyosin superprecipitation was reduced, although the extent was not. 2H2 caused a reduction in the Vmax of both myosin and chymotryptic S1(A1) actin-activated ATPase activity, while the Km appeared to be unaltered. The Mg(2+)-ATPase activity of myosin alone was also unaffected. Binding studies revealed that 2H2 did not prevent the formation of acto-S1 complex, either in the presence or in the absence of ATP, nor did it affect the ability of ATP to dissociate S1 from F-actin. Our findings suggest that the N-terminal region of LC1 is not essential for actin binding but is involved in modulating actin-activated ATPase activity of myosin. | lld:pubmed |
pubmed-article:1533157 | pubmed:language | eng | lld:pubmed |
pubmed-article:1533157 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1533157 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1533157 | pubmed:month | Apr | lld:pubmed |
pubmed-article:1533157 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:1533157 | pubmed:author | pubmed-author:Kendrick-Jone... | lld:pubmed |
pubmed-article:1533157 | pubmed:author | pubmed-author:dos... | lld:pubmed |
pubmed-article:1533157 | pubmed:author | pubmed-author:EverettA WAW | lld:pubmed |
pubmed-article:1533157 | pubmed:author | pubmed-author:SleepJJ | lld:pubmed |
pubmed-article:1533157 | pubmed:author | pubmed-author:BoeyWW | lld:pubmed |
pubmed-article:1533157 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1533157 | pubmed:day | 28 | lld:pubmed |
pubmed-article:1533157 | pubmed:volume | 31 | lld:pubmed |
pubmed-article:1533157 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1533157 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1533157 | pubmed:pagination | 4090-5 | lld:pubmed |
pubmed-article:1533157 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:1533157 | pubmed:meshHeading | pubmed-meshheading:1533157-... | lld:pubmed |
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pubmed-article:1533157 | pubmed:meshHeading | pubmed-meshheading:1533157-... | lld:pubmed |
pubmed-article:1533157 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1533157 | pubmed:articleTitle | Uncoupling of actin-activated myosin ATPase activity from actin binding by a monoclonal antibody directed against the N-terminus of myosin light chain 1. | lld:pubmed |
pubmed-article:1533157 | pubmed:affiliation | Department of Anatomy, University of Sydney, NSW, Australia. | lld:pubmed |
pubmed-article:1533157 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1533157 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1533157 | lld:pubmed |