Butters T D, Hughes R C
Biochim Biophys Acta. 1981 Feb 6;640(3):655-71. doi: 10.1016/0005-2736(81)90096-1.
Plasma membranes have been purified from an established cell line, Mos 20A of Aedes aegypti, and analysed for glycoprotein and polypeptide constituents by isoelectric focusing and sodium dodecyl sulphate polyacrylamide gel electrophoresis. A major glycoprotein of molecular weight 110 000 carrying binding sites for concanavalin A and soybean agglutinin has been purified to homogeneity. Although located on the cell surface, the 110 kdalton glycoprotein is not labelled by lactoperoxidase-catalysed radioactive iodination of whole cells. Analysis indicated the presence of N-glycans, containing on average nine mannose residues, and the N-acetylglucosaminyl-beta 1, 4-N-acetylglucosamine sequence. In addition, O-glycosidically linked N-acetylgalactosamine residues are present.
从埃及伊蚊已建立的细胞系Mos 20A中纯化了质膜，并通过等电聚焦和十二烷基硫酸钠聚丙烯酰胺凝胶电泳分析了其糖蛋白和多肽成分。一种分子量为110 000的主要糖蛋白已被纯化至同质，该糖蛋白带有伴刀豆球蛋白A和大豆凝集素的结合位点。尽管位于细胞表面，但110 kDa的糖蛋白不能通过乳过氧化物酶催化的全细胞放射性碘化进行标记。分析表明存在平均含有九个甘露糖残基的N-聚糖，以及N-乙酰葡糖胺-β1,4-N-乙酰葡糖胺序列。此外，还存在O-糖苷键连接的N-乙酰半乳糖胺残基。
