期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：10
页码：3913-3916
DOI：10.1073/pnas.71.10.3913
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
