Purification and Properties of a Microsomal Enzyme System Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme

Abstract

In this follow-up to an earlier article, Anfinsen, Goldberger, and Epstein reported solubilization and partial purification of the active microsomal protein, and described some of the properties of the soluble system. This and other studies seemed to make clear that the integrity of microsomes as organized particles was not required for catalyzing the reactivation of the reduced forms of ribonuclease and lysozyme. Their findings suggested that the microsomal system might function to facilitate the conversion of at least two different polypeptide chains to the corresponding native proteins during the synthesis of most proteins containing disulfide bonds.