The Kinetics of Formation of Native Ribonuclease During Oxidation of the Reduced Polypeptide Chain
Contributor(s):
Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Sela, Michael
Proceedings of the National Academy of Sciences of the United States of America
Haber, Edgar, 1932-1997
White, F. H., Jr
In this article, Anfinsen, Haber, Sela, and White reported that there existed a considerable lag phase before enzymatic activity appeared after the sample of bovine pancreatic ribonuclease was treated with mercaptoethanol in urea, during which period the sulfhydrl titer and the specific optical rotation changed along a curve similar to that of a first-order reaction. The lag in enzymatic activity in vitro often took several hours, while the same process seemed to take only a few minutes in vivo. This discrepancy eventually led to the discovery of an enzyme system in the endoplasmic reticulum of cells that catalyzes the disulfide interchange reaction, and subsequently, the rapid formation of the correct, native disulfide pairing in relatively short order.
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