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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
A mammalian thioglycosidase.
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A thioglycosidase capable of catalyzing the hydrolysis of 6-purine beta-d-glucothiopyranoside and other thioglycosides has been found in a number of mammalian tissues (including tumors) as well as in almond emulsin. The substrate specificity of mammalian thioglycosidase involves both the aglycone
Characterization of the neutral glycopeptides containing the structure alpha-L-fucopyranosyl-(1 leads to 3)-2-acetamido-2-deoxy-D-glucose from human neuroblastoma cells.
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Human tumor cells of neurectoderm origin contain a high proportion of alpha-L-fucosyl linkages were determined by high-resolution, 500-MHz, 1H-n.m.r. spectroscopy which gave signals characteristic for alpha-L-Fucp-(1 leads to 3)-D-GlcNAc residues these L-fucosyl residues. This was shown by use of a
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