Anion transport in red blood cells and arginine-specific reagents. The location of [14C]phenylglyoxal binding sites in the anion transport protein in the membrane of human red cells.

The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane at pH 7.4 results in complete inhibition of sulfate equilibrium exchange across human red cells. The inactivation was found to be concentration and time dependent. The binding sites of this reagent in the anion transport protein (band 3) under these conditions were determined by using [14C]phenylglyoxal. The rate of incorporation of the radioactivity into band 3 gave a good correlation with the rate of inactivation. Under conditions where the transport is completely inhibited about 6 mol [14C]phenylglyoxal are incorporated into 1 mol band 3. Treating the [14C]phenylglyoxalated ghosts at different degrees of inactivation with extracellular chymotrypsin showed that about two-thirds of these binding sites are located on the 60 kDa fragment.