Fractionation of human red cell membrane proteins by ion-exchange chromatography in detergent on mono Q, with special reference to the glucose transporter

The anion exchanger Mono Q has been used for rapid and efficient fractionation of human red cell membrane proteins in the easily removable detergents n-octyl-β-d-glucopyranoside or nonanoyl-N-methylglucamide. In practice the chromatographic resolution of membrane proteins was lower than for water-soluble proteins, perhaps due to protein—protein interactions and microheterogeneity, but several components, or groups of components, separated well upon salt gradient elution. The glucose transporter (or transportase) was eluted early, glycophorins later, and the anion transporter still later. The detergents Berol 185 and the zwitter-ionic derivatives of cholate, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulphonate and 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-l-propanesulphonate, gave similar chromatographic results but differed in solubilization selectivity.