Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-2-20
pubmed:abstractText
The biosynthesis and the maturation of Thy-1 antigen of mouse thymocytes have been studied by using a xenogeneic rabbit anti-mouse Thy-1 antibody. The earliest form of Thy-1 detected after a 5-min pulse with [35S]methionine and [35S]cysteine had an apparent m.w. of 26,500. During chase, this band converted to a molecular ratio (Mr) = 25,000 polypeptide, probably derived from the latter by trimming of glucose or mannose residues from the three high-mannose glycan units of Thy-1. Mature Thy-1 molecules were detected at the cell surface after a 15-min chase. At least one of the three N-linked oligosaccharide units was shown to be in the high mannose form at the cell surface, as indicated by its susceptibility to endo-beta-N-acetylglucosaminidase H digestion. Treatment of the early and late forms of Thy-1 antigen with endo-beta-N-acetylglucosaminidase F generated a single polypeptide of Mr = 13,500. The same precursor was obtained when cells were labeled in the presence of tunicamycin. This indicates the absence of O-linked glycan in the mature cell surface antigen. Finally, the resistance of Thy-1 antigen to trypsin digestion when associated with membranes confirmed that this molecule has no cytoplasmically oriented portion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1084-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Biosynthesis of mouse Thy-1 antigen.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't