Nonreversibility in the Reductive Denaturation of Chymotrypsinogen A 1

Abstract

Summary

Investigation of the air-reoxidation of denatured, fully reduced chymotrypsinogen A resulted in a maximum recovery of 1.4% of enzymatically active chymotrypsin upon treatment with trypsin. Under the same conditions, urea-denatured chymotrypsinogen, which had not been reduced, yielded 100% recovery of enzymatic activity. Thus the biologically functional conformation of the polypeptide chain comprising chymotrypsinogen may not be that of greatest thermodynamic stability.