Linked Life Data

2449360

Source:http://linkedlifedata.com/resource/pubmed/id/2449360

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-3-25
pubmed:abstractText
The interaction of vinculin with actin filaments was investigated by methods which exclude interference by contaminating proteins which may occur in vinculin preparations. Vinculin which was blotted from SDS-polyacrylamide gels onto nitrocellulose, was stained specifically by fluorescently labeled polymeric actin (100 mM KCl, 2 mM MgCl2). Vinculin which was purified from alpha-actinin and an actin polymerization-inhibiting protein (HA1), was found to be cosedimented with polymeric actin. Maximally one vinculin molecule was cosedimented per one hundred actin filament subunits. Half maximal binding of vinculin was observed at about 0.25 microM free vinculin. Vinculin could be replaced from actin by the addition of tropomyosin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
228
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Evidence for direct binding of vinculin to actin filaments.
pubmed:affiliation
Institute of Physiological Chemistry, Ruhr-University Bochum, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't