Inhibition of anion transport across the red cell membrane by dinitrophenylation of a specific lysine residue at the H2DIDS binding site of the band 3 protein

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Abstract
The inhibition of anion transport by dinitrophenylation of the red cell membrane is brought about by the modification of a single lysine residue located on the 17‐kDa segment of the band 3 protein. This residue is identical with Lys a, which is also capable of reacting with one of the two isothiocyanate groups of 4,4'‐diisothiocyano dihydro‐stilbene‐2,2'‐disulfonate (H2DIDS). The rate of reaction between Lys a and 1‐fluoro‐2,4‐dinitrobenzene is reduced when a second lysine residue on the 35‐kDa segment of the band 3 protein becomes dinitrophenylated. This latter residue is not identical with Lys b which is known to be present on the 35‐kDa segment and involved in the cross‐linking of this segment with the 17‐kDa segment by H2DIDS.

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