Linked Life Data

8135824

Source:http://linkedlifedata.com/resource/pubmed/id/8135824

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-4-21
pubmed:abstractText
Myosin light chain kinase has an inhibitory effect on the interaction of actin filaments with phosphorylated smooth muscle myosin. Myosin light chain kinase binds to actin filaments, and the inhibition is attributable to the actin-binding activity and not the kinase activity of myosin light chain kinase [Kohama et al. (1992) Biochem. Biophys. Res. Commun. 184, 1204-1211]. We now report that myosin light chain kinase is able to assemble actin filaments into thick bundles, which can be visualized by optical and electron microscopy and can be monitored by measuring the sedimentation and flow birefringence of actin filaments. The bundling activity of myosin light chain kinase is abolished by calmodulin in the presence of Ca2+. The possibility is discussed that myosin light chain kinase has multiple actin-binding sites through which it can cross-link actin filaments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
199
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
786-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Bundling of actin filaments by myosin light chain kinase from smooth muscle.
pubmed:affiliation
Department of Pharmacology, Gunma University School of Medicine, Maebashi, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't