作者: Charles H. Schmelzer , Shirley E. Poduslo
DOI: 10.1016/0005-2736(87)90160-X
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摘要: Two glycoproteins of 99 kDa and 77 which exhibit intense binding to wheat germ agglutinin have been purified from the whorls membrane produced by oligodendroglia in culture. The were isolated gradient centrifugation bovine maintained two solubilized membranes using a non-ionic detergent Sephadex LH-60 chromatography, affinity SDS-polyacrylamide pore gel electrophoresis. HPLC peptide mapping 99-kDa 77-kDa revealed structural differences between proteins. Peptide suggested that glycoprotein may be homologous plasma membranes. both sets also structurally related. Lectin studies showed bound agglutinin, succinylated concanavalin A, lentil lectin, indicating presence high mannose hybrid type oligosaccharide side-chains.