Purification and Properties of a Microsomal Enzyme System Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme Microsomes Ribonucleases Enzymes Oxidation-Reduction Research Design In this follow-up to an earlier article, Anfinsen, Goldberger, and Epstein reported "the 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. American Society for Biochemistry and Molecular Biology, 1964 The American Society for Biochemistry and Molecular Biology, 1964 Journal of Biological Chemistry Goldberger, Robert Epstein, Charles Anfinsen, Christian B. Anfinsen, Christian B. Articles Archival Materials Text 5 pages nlm:nlmuid-101584571X145-doc 101584571X145 http://resource.nlm.nih.gov/101584571X145 Profiles ID: KKBBJY English Profiles in Science