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- W2074408061 abstract "SUMMARY. The human erythrocyte membrane contains four sialoglycoproteins, denoted α, β, γ and δ (also known as glycophorins A, C, D and B respectively), of which α‐sialoglycoprotein (α‐SGP) is the most predominant species. The extracellular portion of α‐SGP is heavily glycosylated with approximately 15 O‐linked carbohydrate side‐chains and a single N ‐linked group. We have used inhibitors of carbohydrate trimming enzymes to investigate the contribution of this single N ‐glycan moiety towards the recognition of a range of antibody binding sites on α‐SGP. Two erythromyeloid cell lines, K562 and HEL, were cultured in the presence of these inhibitors and altered binding of antibodies to epitopes adjacent to the N ‐glycan was observed. Digoxigenin‐coupled lectins were used to stain cytocentrifuge preparations and Western blots of cell lysates in order to confirm that modification of N ‐linked carbohydrate side‐chains had been achieved. We suggest that the N ‐glycan side chain of α‐SGP has a role in conferring conformational stability upon epitopes which lie in its vicinity." @default.
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- W2074408061 date "1992-03-01" @default.
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- W2074408061 title "The effect of glycosylation trimming enzyme inhibitors on monoclonal antibody recognition of α-sialoglycoprotein epitopes" @default.
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- W2074408061 doi "https://doi.org/10.1111/j.1365-3148.1992.tb00130.x" @default.
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