Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-4-15
pubmed:abstractText
Vinculin prepared by published procedures (i.e., Feramisco, J. R., and K. Burridge, 1980, J. Biol. Chem., 255:1194-1199) contains contaminants that have been shown by Evans et al. (Evans, R. R., R. M. Robson, and M. H. Stromer, 1984, J. Biol. Chem., 259:3916-3924) to reduce the low-shear viscosity of F-actin solutions. In this study we separated contaminants from conventional vinculin preparations by hydroxylapatite chromatography. We found that although the contaminants represented a small fraction (less than or equal to 5%) of the total protein in the conventional vinculin preparations, they were responsible for practically all of the filament capping and bundling activities previously attributed to vinculin. In addition, we examined the size of the molecule(s) responsible for the observed capping activity and found that its apparent molecular weight under denaturing conditions in sodium dodecyl sulfate (SDS) polyacrylamide gels fell within a broad range of 23,000-33,000. These results contrast with the observation that under nondenaturing conditions, the activity migrated in gel filtration columns at a position that corresponded to the Stoke's radius of a much bigger molecule. Since the migration of the activity in these chromatographic experiments is independent of the presence of vinculin, it is unlikely that the active protein associates with vinculin with high affinity under the conditions examined.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-287078, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-3919032, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-3972790, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-3994988, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-4254541, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-574428, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6323447, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6650826, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6789327, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6802502, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6809402, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6809403, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6811758, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6863518, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-6892818, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-7356657, http://linkedlifedata.com/resource/pubmed/commentcorrection/3005334-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1085-92
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
A re-examination of the interaction of vinculin with actin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.