It is shown that there are spasmodic changes of electroconductivity in bimolecular membranes in the presence of alpha-chimotripsin and denatured ovalbumin or glycyl-d,L-beta-phenylalanine. These conductivity changes are not due to the interaction ob proteolysis products with lipid bilayer but result from the interaction of alpha-chimo trypsin with the substrate or competing inhibitor. Probability of the state with a specific conductivity depends on the membrane voltage. A modified membrane has a low ionic selectivity.
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