Linked Life Data

9397525

Source:http://linkedlifedata.com/resource/pubmed/id/9397525

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1998-1-7
pubmed:abstractText
The in vitro motility of fluorescent actin filaments over heavy meromyosin (HMM) was studied in the presence of the nonionic detergent Triton X-100. Below 0.004% Triton X-100 concentration, motility was not affected. Above 0.007%, motility was not observed because actin filaments were dissociated from HMM. In the Triton X-100 concentration range of 0.004-0.007%, the sliding actin filaments dissociated from HMM with a delay. The dissociation delay time decreased with increasing Triton X-100 concentration, increasing ATP (adenosine-5'-triphosphate) concentration, and increasing temperature. The delayed acto-HMM dissociation was absent when weak-binding kinetic intermediates of the myosin ATPase cycle (M.ATP and M.ADP-Pi) were used. The presence of sliding movement was necessary to evoke the delayed acto-HMM dissociation. The acto-HMM dissociation delay was independent of actin filament length. For a given Triton X-100 concentration, the dissociation delay time was found to be inversely proportional to sliding velocity, indicating that actin filaments travel a more or less constant distance prior to dissociation from HMM. The actin-activated HMM ATPase activity was not inhibited by Triton X-100; rather, it was slightly enhanced. The results imply the presence of a motility-associated conformational change in acto-HMM.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-210
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Delayed dissociation of in vitro moving actin filaments from heavy meromyosin induced by low concentrations of Triton X-100.
pubmed:affiliation
Central Laboratory, University Medical School of Pécs, Hungary. keller@wsu.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't