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. 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

S P Grefrath, J A Reynolds

The molecular weight of the major glycoprotein from the human erythrocyte membrane

S P Grefrath et al. Proc Natl Acad Sci U S A. 1974 Oct.

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.

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