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2 results
Stable oligosaccharide microheterogeneity at individual glycosylation sites of a murine major histocompatibility antigen derived from a B-cell lymphoma.
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The H-2Kk glycoprotein has been isolated by monoclonal antibody affinity chromatography, and an analysis of the asparagine-linked oligosaccharides present at the two major glycosylation sites has been performed. Antigen obtained from the AKTB-1b B-cell lymphoma that had been labeled with
Lymphocyte function-associated antigen 1 (LFA-1) contains sulfated N-linked oligosaccharides.
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The murine lymphocyte function-associated antigen 1 (LFA-1) is a glycoprotein heterodimer consisting of an Mr 180,000 alpha-chain and an Mr 95,000 beta-chain. Although LFA-1 has been studied extensively in the past few years due to its involvement in various antigen-specific T lymphocyte responses,
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