IDENTIFICATION OF LIVER PLASMA-MEMBRANE GLYCOPROTEINS WHICH BIND TO I-125-LABELED CONCANAVALIN-A FOLLOWING ELECTROPHORESIS IN SODIUM DODECYL-SULFATE
IDENTIFICATION OF LIVER PLASMA-MEMBRANE GLYCOPROTEINS WHICH BIND TO I-125-LABELED CONCANAVALIN-A FOLLOWING ELECTROPHORESIS IN SODIUM DODECYL-SULFATE
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DOI：
10.1139/o76-068
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发表时间：
1976-01-01
期刊：
影响因子：
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通讯作者：
EVANS, WH
中科院分区：
文献类型：
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作者：
GURD, JW;EVANS, WH
在十二烷基硫酸钠（SDS）中对卵白蛋白进行电泳后发现，该糖蛋白结合了125i标记的豆豆蛋白A （Con A）。反应是特异性的，与凝胶上糖蛋白的量成正比。该技术用于肝细胞表面con - a结合糖蛋白的研究。小鼠肝质膜经纯化和分离得到胆小管表面和相邻肝细胞间表面对应的2个部分。两个组分结合125i标记的Con A，前者结合的凝集素是后者的2-3倍。SDS凝胶电泳后，单个膜糖蛋白与125i标记的Con A反应，两种膜亚组分得到了质量相似的Con A结合谱，每种膜亚组分都存在7种结合蛋白。结果与糖蛋白在肝细胞表面的均匀分布一致。SDS凝胶电泳后凝集素与糖蛋白的反应在膜组成的研究中具有普遍的应用价值。
Following electrophoresis of ovalbumin in sodium dodecyl sulfate (SDS) this glycoprotein bound 125I-labeled Concanavalin A (Con A). The reaction was specific and proportional to the amount of glycoprotein present on the gel. This technique was used to study the Con-A-binding glycoproteins of liver cell surfaces. Mouse liver plasma membranes were purified and subfractionated to yield 2 fractions corresponding to the bile canalicular surface and the surface between adjacent hepatocytes. Both fractions bound 125I-labeled Con A, the former binding 2-3 times more lectin than the latter. Following SDS gel electrophoresis individual membrane glycoproteins reacted with 125I-labeled Con A. Both membrane subfractions yielded qualitatively similar Con A binding profiles, 7 binding proteins being present in each. The results are consistent with a generally uniform distribution of glycoproteins over the hepatocyte surface. The reaction of lectins with glycoproteins following SDS gel electrophoresis should find general application in the study of membrane composition.