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Abstract

The transport properties of the Ca‐activated, K channel in the resealed human red blood cell ghost can be modified by the action of incorporated trypsin. Membranes were maximally depleted of diffusible cytoplasmic components by hemolysis on a gel filtration column at 0 °C. Subsequently, isotonicity was restarted and 0.01–1 μg/ml trypsin incorporated. Partial digestion of the membrane proteins occurred during reselling. As the degree of tryptic digestion increased, the channel became initially permeable to K and later to both K and Na; and then the channel became refractory to the action of applied Ca. The observations suggest that tryplic digestion of proteins at the inner membrane surface leads to modifications of the selectivity filter and the Ca‐receptor site of the channel. The modifications probably stem from alterations at the inner surface of a trans membrane protein which acts as a channel. Under conditions where selectivity is lost, the channel is still inhibited by externally applied TbCl₃.