Purification and Properties of a Microsomal Enzyme System Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme
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.
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Anfinsen, Christian B.
Periodical: Goldberger, Robert, Charles Epstein, and Christian B. Anfinsen. "Purification and Properties of a Microsomal Enzyme System
Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme." Journal of Biological Chemistry 239, 5 (1964): 1406-1410.
Article. 5 Images.
American Society for Biochemistry and Molecular Biology
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.