Enhancement of anion permeability in lecithin vesicles by hydrophobic proteins extracted from red blood cell membranes

Triton X-100 extracts of membrane proteins from ghosts of normal and pronase treated cells enhance the anion permeability of lecithin vesicles. With proteins from cells pretreated with DIDS (4,4′-diisothiocyano-2,2′-stilbene disulfonate), a specific inhibitor of anion transport, the anion permeability is not enhanced. On the basis that the Triton X-100 extracts are considerably enriched in a protein component of 95,000 molecular weight (or a 65,000 molecular weight segment in the case of pronase treated cells), and that DIDS is bound almost exclusively to the same proteins, it is suggested that the pronase resistant, 65,000 molecular weight segment of the 95,000 molecular weight protein is directly involved in anion transport.