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Science 10 March 1978:
Vol. 199. no. 4333, pp. 1084 - 1087
DOI: 10.1126/science.564548
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Articles

Science, Vol 199, Issue 4333, 1084-1087
Copyright © 1978 by American Association for the Advancement of Science

articles

Enhancement of bovine pancreatic ribonuclease activity by mercaptoethanol

JB Watkins and FW Benz

Incubation of ribonuclease with 0.1M mercaptoethanol at pH 8.5 can increase the enzyme's hydrolytic activity toward cytidine 2',3'-monophosphate (cyclic CMP) under standard assay conditions. Cation-exchange chromatography of the ribonuclease-thiol reaction mixture revealed seven fractions. The fraction with the highest activity had an approximate tenfold decrease in the apparent Michaelis constant for cyclic CMP with respect to native ribonuclease. The enhanced activity is a metastable property since this fraction reverts back to the control activity and chromatographic behavior of native ribonuclease on standing in solution at room temperature.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)