The monosaccharide transporter of the human erythrocyte. Transport activity upon reconstitution.

摘要: The transport function of the purified monosaccharide transporter from human erythrocytes has been investigated. By a cycle cholate solubilization and removal, was incorporated into phospholipid vesicles about 300 A diameter, at density one per vesicle. This distribution permitted an all-or-none assay for activity, in which fraction intravesicular volume that rapidly equilibrated with D-glucose medium yielded estimate moles protein functional transport. It found almost every molecule capable binding cytochalasin B also rate transporter-catalyzed exchange between equilibrium measured. In this assay, activity protein, expressed mol site, 5% intact erythrocyte under similar conditions. These results show reduced various assays is due to most molecules functioning lower rate, rather than few vivo rate.