Linked Life Data

161509

Source:http://linkedlifedata.com/resource/pubmed/id/161509

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
1980-6-25
pubmed:abstractText
Whereas dissociation of rabbit skeletal muscle myosin light chains occurs at an increased temperature (25 degrees) and in the absence of divalent cations, reassociation of the myosin oligomer requires a low temperature (4 degrees C) and the presence of divalent cations, thus resulting in the original light to heavy chain stoichiometry. With a 5-10 per cent release of alkali light chains, LC1 and LC3, and a 50 per cent dissociation of the Ca2+ binding light chain, LC2, there is no significant decrease in myosin ATPase activity irrespective of the cation activator, however, there is an approximate 15-20 per cent decrease in actomyosin ATPase activity. With reassociation of the myosin oligomer, actomyosin ATPase activity is partially restored as well as the original number of Ca2+ binding sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1309-14
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Dissociation and reassociation of rabbit skeletal muscle myosin.
pubmed:publicationType
Journal Article