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Band 3 and glucose transport protein (GluTl) are two kinds of important proteins in the human erythro-cyte membranes. Bis(sulfosuccinimidyl)suberate (BS ), an impermeable cross-linker of band 3, inhibited NO2- transport, showing that anion exchange is affected by the association state of band 3 in the intact erythrocyte membranes. At the same time, the rates of glucose transport of both exit and entry declined. The amount of monomers of band 3 was decreased after treatment of the erythrocytes with BS3, but there was no change in GluTl according to the SDS-PAGE patterns. This demonstrates that band 3 and GluTl would be linkaged together in the erythrocyte membranes for the requirement of rapid and cooperative performance of physiological functions of the membrane proteins.
Bis (sulfosuccinimidyl) suberate (BS), an impermeable cross-linker of band 3, inhibited NO2-transport, showing that anion exchange is affected by the association state of band 3 in the intact erythrocyte membranes. At the same time, the rates of glucose transport of both exit and entry declined. The amount of monomers of band 3 was decreased after treatment of the erythrocytes with BS3, but There was no change in GluTl according to the SDS-PAGE patterns. This demonstrates that band 3 and GluTl would be linkaged together in the erythrocyte membranes for the requirement of rapid and cooperative performance of physiological functions of the membrane proteins.