Grefrath S P, Reynolds J A
Proc Natl Acad Sci U S A. 1974 Oct;71(10):3913-6. doi: 10.1073/pnas.71.10.3913.
The molecular weight of the major glycoprotein from the human erythrocyte membrane is 29,000, of which 55% is carbohydrate and 45% is protein. The binding of sodium dodecyl sulfate to this glycoprotein is anomalous when compared to water soluble proteins and leads to migration rates in sodium dodecyl sulfate-polyacrylamide gels that cannot be interpreted in terms of molecular weight. Anomalous sodium dodecyl sulfate binding may be a general characteristic of many intrinsic membrane proteins even if they are not glycoproteins, and such proteins are likely to have mobilities in sodium dodecyl sulfate-gel electrophoresis that do not correspond to the mobilities of water soluble proteins of identical molecular weight.
人红细胞膜主要糖蛋白的分子量为29,000,其中55%为碳水化合物,45%为蛋白质。与水溶性蛋白质相比,十二烷基硫酸钠与这种糖蛋白的结合是异常的,这导致其在十二烷基硫酸钠-聚丙烯酰胺凝胶中的迁移率无法用分子量来解释。异常的十二烷基硫酸钠结合可能是许多内在膜蛋白的普遍特征,即使它们不是糖蛋白,并且这类蛋白在十二烷基硫酸钠-凝胶电泳中的迁移率可能与相同分子量的水溶性蛋白的迁移率不对应。