Abstract
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.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 2:48 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:40 a.m.) |
Indexed | 2 months ago (July 2, 2025, 5:18 a.m.) |
Issued | 50 years, 11 months ago (Oct. 1, 1974) |
Published | 50 years, 11 months ago (Oct. 1, 1974) |
Published Online | 50 years, 11 months ago (Oct. 1, 1974) |
Published Print | 50 years, 11 months ago (Oct. 1, 1974) |
@article{Grefrath_1974, title={The Molecular Weight of the Major Glycoprotein from the Human Erythrocyte Membrane}, volume={71}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.71.10.3913}, DOI={10.1073/pnas.71.10.3913}, number={10}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Grefrath, Stuart P. and Reynolds, Jacqueline A.}, year={1974}, month=oct, pages={3913–3916} }