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. 1972 Sep;129(2):333–347. doi: 10.1042/bj1290333

Separation and some properties of the major proteins of the human erythrocyte membrane

M J A Tanner 1, D H Boxer 1
PMCID: PMC1174083  PMID: 4643321

Abstract

A fractionation procedure is described which allows the isolation of three major human erythrocyte membrane proteins. Their isolation involves three sequential extraction procedures followed by gel filtration in 1% sodium dodecyl sulphate and preparative gel electrophoresis. All three proteins can be isolated from a single preparation. One of the proteins is the erythrocyte sialoglycoprotein, for which no C- or N-terminal residues were found. The other two proteins, which have not previously been isolated, have subunit molecular weights of 74000 and 93000 and contain 9 and 7% carbohydrate respectively. These glycoproteins have blocked N-terminal residues and show similarities in their chemical properties. Preparations derived from blood-group O erythrocytes contain no N-acetylgalactosamine, but similar preparations from blood-group A erythrocytes do contain this sugar. These three proteins cannot easily be solubilized by gentle aqueous procedures and represent about half of the erythrocyte `ghost' protein. They carry a large proportion of the cell-surface carbohydrate.

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Selected References

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