Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-12-18
pubmed:abstractText
Human breast carcinoma contains high-affinity receptors for the basement membrane glycoprotein laminin. Plasma membranes isolated from tissue samples of human breast carcinoma exhibit specific, saturable, reversible, and displaceable binding to laminin. Fibronectin, collagen, and serum proteins fail to displace this bound laminin. Scatchard analysis is linear with a Kd of 1.8 X 10(-9) M. The laminin receptor, isolated and purified 1200-fold by laminin-affinity chromatography, exhibits a molecular weight of 67 000 daltons as determined by gel electrophoresis. The receptor was verified to be located on the cell surface of the invading breast carcinoma cells by immunohistologic studies utilizing a peroxidase-conjugated fragment of the laminin molecule which contained the receptor-binding domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0167-6806
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Characterization of a laminin receptor from human breast carcinoma tissue.
pubmed:publicationType
Journal Article