Linked Life Data

3158744

Source:http://linkedlifedata.com/resource/pubmed/id/3158744

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1985-7-15
pubmed:abstractText
Readdition of regulatory light chains to regulatory light chain denuded scallop myofibrils, in the presence of magnesium, results in a negatively co-operative restoration of calcium sensitivity as a function of regulatory light chain content. The form of the stoichiometry curves obtained in the presence of 10 mM-EDTA, by light chain removal from scallop myofibrils at various temperatures, are parabolic in shape, consistent with a random removal process. However, in the presence of EDTA at low temperatures, regulatory light chains are removed in a biphasic manner, indicating that the binding constants of the light chains for each myosin head are not equivalent under these conditions. It is shown here that as the temperature is raised, light chain removal by EDTA approaches that of a random process. The stoichiometry curves obtained in the presence of 10 mM-EDTA may therefore be seen as a composite of both a biphasic removal process (temperatures below 20 degrees C) and a random removal process (temperatures above 20 degrees C), there being a temperature-dependent switch in the myosin molecule between 17 and 23 degrees C that governs the mode of light chain removal. These results indicate that both myosin heads must contain light chains for calcium sensitivity and are consistent with our earlier proposals for head-head co-operativity within the scallop myosin molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
557-60
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Regulatory light chains and scallop myosin. Form of light chain removal or reuptake is dependent on the presence of divalent cations.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't