Band 3 and glucose transport protein (GluT1) are two kinds of important proteins in the human erythrocyte membranes. Bis(sulfosuccinimidyl)suberate (BS3), 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 GluT1 according to the SDS-PAGE patterns. This demonstrates that band 3 and GluT1 would be linkaged together in the erythrocyte membranes for the requirement of rapid and cooperative performance of physiological functions of the membrane proteins.