THE DENATURATION OF COVALENTLY INHIBITED SWINE PEPSIN

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Abstract
Studies are reported on the denaturation of freshly prepared, intact swine pepsin, which was inactivated by reaction with diazoacetylglycine ethyl ester, to prevent autolysis. Denaturation about pH 6 involved a small expansion of the molecular domain with some loss of organized secondary structure. Increasing concentrations of guanidine hydrochloride induced cooperative transitions in both the native and alkali denatured forms to give a cross-linked random coil. No conditions were found in which these reactions were reversible. Removal of denaturing conditions usually resulted in aggregation and precipitation of protein. It would seem that the active conformation is largely predetermined in the zymogen.