Purification and characterization of two glycoproteins from oligodendroglial plasma membranes.
Purification and characterization of two glycoproteins from oligodendroglial plasma membranes.
复制标题
少突胶质细胞质膜中两种糖蛋白的纯化和表征。
DOI：
10.1016/0005-2736(86)90291-9
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发表时间：
1986
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
从少突胶质细胞质膜中提纯了99 kDa和77 kDa两种主要糖蛋白。这两种糖蛋白与小麦胚芽凝集素凝集素有很强的结合。用Sephadex LH-60柱层析、麦胚凝集素亲和层析和SDS-聚丙烯酰胺孔梯度凝胶电泳法对99 kDa和77 kDa糖蛋白进行了纯化。含有这两种糖蛋白的凝胶切片的再电泳法显示它们明显是均一的。99 kDa和77 kDa糖蛋白的等电点分别为6.15和6.00。肽图谱显示了两种糖蛋白之间的结构差异。用放射性标记的琥珀酸化小麦胚凝集素与凝集素结合的研究表明，99 kDa和77 kDa糖蛋白与小麦胚凝集素的结合是由于寡糖侧链上的N-乙酰-d-氨基葡萄糖残基所致。
Two major glycoproteins of 99 kDa and 77 kDa have been purified from oligodendroglial plasma membranes. These two glycoproteins exhibit intense binding to the lectin, wheat germ agglutinin. The 99-kDa and 77-kDa glycoproteins were purified by Sephadex LH-60 chromatography, wheat germ agglutinin affinity chromatography and SDS-polyacrylamide pore gradient gel electrophoresis. Re-electrophoresis of excised gel slices containing the two glycoproteins demonstrated their apparent homogeneity. The isoelectric points of the 99-kDa and 77-kDa glycoproteins were 6.15 and 6.00, respectively. Peptide mapping revealed structural differences between the two glycoproteins. Lectin binding studies with radiolabeled succinylated wheat germ agglutinin demonstrated that the binding of the 99-kDa and 77-kDa glycoproteins to wheat germ agglutinin was due to N-acetyl-d-glucosamine residues in the oligosaccharide side-chains.