Drzeniek Z, Lisowska E
Arch Immunol Ther Exp (Warsz). 1979;27(1-2):263-70.
Human erythrocyte membranes and the glycoprotein isolated by phenol-water extraction of membranes were fractionated by gel filtration on Bio-Gel P-300 in 1% SDS. It was shown by this procedure that lipids (and possibly other membrane components) promote the dissociation of glycoprotein aggregates in SDS-containing solutions. The isolated glycoprotein gives several fractions on gel filtration in 1% SDS. The main fraction contains the major sialogylcoprotein (MN), which can be obtained in an electrophoretically homogeneous form (PAS-1) when only a part of the major peak is pooled and re-chromatographed. The purified glycoprotein has elevated MN blood group activity, does not show I activity, and contains components of alkalibabile oligosaccharide chains in slightly higher proportion than crude glycoprotein. The other fractions have distinctly different carbohydrate composition and contain glycoproteins of different electorphoretic mobility in SDS-PAGE.
人红细胞膜以及通过膜的酚 - 水提取法分离得到的糖蛋白,在1%十二烷基硫酸钠(SDS)存在下,于Bio - Gel P - 300上进行凝胶过滤分级分离。通过该程序表明,脂质(以及可能的其他膜成分)促进含SDS溶液中糖蛋白聚集体的解离。分离得到的糖蛋白在1% SDS中进行凝胶过滤时产生几个级分。主要级分包含主要的唾液酸糖蛋白(MN),当仅合并主峰的一部分并重新层析时,可获得电泳纯形式(PAS - 1)。纯化的糖蛋白具有升高的MN血型活性,不显示I活性,并且与粗糖蛋白相比,其碱不稳定寡糖链成分的比例略高。其他级分具有明显不同的碳水化合物组成,并且在SDS - 聚丙烯酰胺凝胶电泳(SDS - PAGE)中含有不同电泳迁移率的糖蛋白。