Glycoproteins in the whorls of membrane produced by oligodendroglia in culture.
Glycoproteins in the whorls of membrane produced by oligodendroglia in culture.
复制标题
培养物中少突胶质细胞产生的膜轮中的糖蛋白。
DOI：
10.1016/0005-2736(87)90160-x
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Poduslo,SE
中科院分区：
文献类型：
--
作者：
Schmelzer,CH;Poduslo,SE
从培养的少突胶质细胞产生的膜上分离得到了与小麦胚芽凝集素结合较强的2个糖蛋白，分别为99 kDa和77 kDa。用梯度离心法从牛少突胶质细胞中分离出膜的螺旋。用非离子洗涤剂将两种糖蛋白从膜上溶解，并通过Sephadex LH-60层析、小麦胚芽凝集素亲和层析和sds -聚丙烯酰胺孔梯度凝胶电泳进行纯化。99-kDa和77-kDa糖蛋白的HPLC肽图谱显示了两种蛋白之间的结构差异。肽图谱显示，来自膜旋体的99-kDa糖蛋白可能与来自质膜的糖蛋白同源。来自两组膜的77-kDa糖蛋白也可能在结构上相关。凝集素结合研究表明，来自膜轮的两种糖蛋白都与小麦胚芽凝集素、琥珀酰化的小麦胚芽凝集素、豆豆蛋白A和扁豆凝集素结合，表明存在高甘露糖和杂交型低聚糖侧链。
Two glycoproteins of 99 kDa and 77 kDa which exhibit intense binding to wheat germ agglutinin have been purified from the whorls of membrane produced by oligodendroglia in culture. The whorls of membrane were isolated by gradient centrifugation from purified bovine oligodendroglia maintained in culture. The two glycoproteins were solubilized from the membranes using a non-ionic detergent and purified by Sephadex LH-60 chromatography, wheat germ agglutinin affinity chromatography, and SDS-polyacrylamide pore gradient gel electrophoresis. HPLC peptide mapping of the 99-kDa and 77-kDa glycoproteins revealed structural differences between the two proteins. Peptide mapping suggested that the 99-kDa glycoprotein from the whorls of membrane may be homologous to that from the plasma membranes. The 77-kDa glycoproteins from both sets of membrane may also be structurally related. Lectin binding studies showed that both glycoproteins from the whorls of membrane bound to wheat germ agglutinin, succinylated wheat germ agglutinin, concanavalin A, and lentil lectin, indicating the presence of high mannose and hybrid type oligosaccharide side-chains.