Abstract
The use of a strictly identical procedure for the purification of the human erythrocyte Cl −-dependent arginine aminopeptidase (EC 3.4.11.6) separately from 10 healthy adults resulted in enzymes which showed considerable variance in substrate specificity, values of the inhibition constant of p-chloromercuribenzoate, reaction velocities, and degree of substrate inhibition, although the purified enzymes were immunologically identical. These differences were considered to reflect changes in enzyme conformation. The present data were regarded as new because other (polymorphic) peptidases of human erythrocytes previously described differ from the present Cl −-dependent arginine aminopeptidase by virtue of substrate specificity.
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