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Abstract:
Rainbow trout (Salmo gairdneri) band‐3 protein was isolated from trout erythrocyte plasma membranes by a combination of preparative SDS/PAGE and electroelution. High purity and recovery of the plasma membranes were achieved by a new method. This was demonstrated using 4,4′ diiso‐thiocyano[3H2]dihydro‐stilbene 2,2′disulfonic acid (3H2DIDS) which specifically labels band‐3 protein. On SDS/PAGE, band‐3 protein yields a similarly diffuse pattern, as does mammalian band‐3 protein, with an apparent Mr of 116000. In situ chymotryptic cleavage/cross‐linking experiments with 3H2DIDS reveal that the fragments cross‐link as in human and mouse band‐3 proteins but that there are minor differences. Treatment of trout erythrocytes with trypsin results in cleavage of the band‐3 protein. Purified polyclonal antibodies raised against trout band‐3 protein react with trout band‐3 protein and do not crossreact with mouse or human band‐3 protein. They react specifically with only one chymotryptic fragment of trout band‐3 protein.
