Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1985-1-25
pubmed:abstractText
The technique of vectorial labeling has been used to study the orientation of the rat and chicken receptors for asialo- and agalactoglycoproteins in hepatocyte membranes. The membrane-impermeant enzyme lactoperoxidase was used to radioiodinate the outer surfaces of intact cells and endocytic vesicles, as well as both sides of total microsomal membranes. Proteolytically and chemically produced fragments of the receptor polypeptides were analyzed to identify the tyrosine residues modified in each case. The results reveal that each of these receptors is a transmembrane glycoprotein arranged with its NH2 terminus facing the cytoplasm and its COOH terminus, containing the carbohydrate-binding site, exposed at the cell surface. While the primary structures of the chicken and rat receptors are highly homologous in the extracellular portions of the proteins, the cytoplasmic domains show no sequence similarity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15440-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Direct evidence for the transmembrane orientation of the hepatic glycoprotein receptors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't