Erythrocyte membrane proteins: Their study using aqueous pyridine solutions

doi:10.1016/0005-2736(70)90086-6

Biochimica et Biophysica Acta (BBA) - Biomembranes

Volume 211, Issue 2, 7 August 1970, Pages 109-123

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Abstract

1.
1. A new method for the study of membrane proteins is described. It involves the use of aqueous pyridine which permits the separation of proteins of human erythrocyte membrane into two fractions: one water soluble and lipid free the other a water-insoluble lipoprotein. Both fractions show multiple bands on gel electrophoresis and the band patterns of the two fractions and the intact membrane are similar. They suggest a close relationship of the proteins of the two fractions in spite of differences in lipid affinity. The sialoglycoprotein, containing the virus receptor activity, is present uniquely in the water-soluble fraction and its isolation is described.
2.
2. The water-soluble proteins show a strong tendency for association. Such aggregation is promoted by certain salts. Aggregates of various sizes are still present in 33% aqueous pyridine and they can be resolved and visualised by gel electrophoresis in 0.1% sodium dodecyl sulfate as outlined by Shapiroet al.²² into about twenty protein bands of a wide range of molecular weights. Certain proteins of the water-soluble fraction are not present as components of these aggregates. They include a sialoglycoprotein and three other proteins which can be visualized as distinct bands on polyacrylamide gels.

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Erythrocyte membrane proteins: Their study using aqueous pyridine solutions

Abstract

J. Biol. Chem.

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Biochim. Biophys. Acta

J. Biol. Chem.

Biochem. Res. Commun.

Arch. Biochem. Biophys.

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Arch. Biochem. Biophys.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Biochim. Biophys. Acta