Linked Life Data

139917

Source:http://linkedlifedata.com/resource/pubmed/id/139917

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1977-6-30
pubmed:abstractText
Filamin, a major high-molecular-weight protein of chicken gizzard smooth muscle, was purified to homogeneity by salt extraction, ammonium sulfate precipitation, agarose gel filtration, and diethylaminoethylcellulose ion-exchange chromatography. Purified filamin is an asymmetric oligomer consisting of two large subunits of identical size (2 X 250 000 daltons) as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, chemical cross-linking, sedimentation analysis (s10, wo = 10S) and Stokes'radius estimation (a = 120 A), It has no intersubunit disulfide but appears from oxidation studies to have adjacent thiols near the subunit interface. Filamin contains no amino sugars, methylated lysine, methylated histidine, or hydroxyproline, nor does it exhibit myosin-like ATPase activities. Its amino acid composition and physical properties differ from those of gizzard myosin, for which a pruification procedure is described. Filamin and the protein spectrin of erythrocyte membranes have strikingly similar physical properties, but they are chemically distinct.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1857-65
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purification and properties of chicken gizzard filamin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.