On the Stabilization of Ribonuclease S-Protein by Ribonuclease S-Peptide

Rapid scrambling of the disulfide bonds of RNase S-protein, with concomitant inactivation of potential RNase activity, occurs during catalysis by the disulfide interchange enzyme of microsomes. RNase S-peptide prevents this interchange reaction. The enzymically scrambled S-protein is reactivated on the addition of S-peptide and interchange enzyme.