Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-12-22
pubmed:abstractText
This paper describes the isolation and partial characterization of a collagen cell attachment protein from the spent culture medium of rat hepatoma cells. When compared with serum fibronectin, this attachment protein differed in several biochemical parameters. The hepatoma attachment protein was partially purified by adsorbing and eluting from an inorganic gel, magnesium oxide. Cell adhesive activity may routinely recovered at levels of 10 to 30%, and a 2000-fold purification was attained. The hepatoma attachment protein was shown to be sensitive to trypsin and chymotrypsin, to be heat inactivated at 61 degrees, to have a molecular weight of 58,000, to have an isoelectric point of 4.1, to show an electrophoretic mobility on cellulose acetate of approximately one-half that of fibronectin, and not to cross-react with antifibronectin antisera.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4027-30
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Collagen cell attachment protein from rat hepatoma cells.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.