Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1990-10-18
pubmed:abstractText
Endothelial cell CD36 (glycoprotein IV) has been purified from bovine heart tissue by detergent partitioning and immunoaffinity chromatography. Bovine CD36 differs from human CD36 in its apparent mass (85 versus 88 kDa), primary structure, and immunological cross-reactivity. Of the 18 N-terminal residues identified, 17 conformed to the human CD36 sequence. Mouse monoclonal antibodies E-1 and 8A6 defined bovine- and human-specific epitopes, respectively. Because human CD36 has been identified as a receptor for erythrocytes infected with the malaria parasite Plasmodium falciparum, we examined the ability of bovine CD36 to bind infected erythrocytes. Bovine CD36, unlike human CD36, did not bind infected erythrocytes, suggesting that human CD36-specific structural features are responsible for recognition of the infected erythrocyte ligand.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16296-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structural, functional, and antigenic differences between bovine heart endothelial CD36 and human platelet CD36.
pubmed:affiliation
Department of Chemistry, San Jose State University, California 95192-0101.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't