Enhancement of bovine pancreatic ribonuclease activity by mercaptoethanol

John B. Watkins, F. W. Benz

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Incubation of ribonuclease with 0.1 M 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 ofnative ribonuclease on standing in solution at room temperature.

Original languageEnglish (US)
Pages (from-to)1084-1087
Number of pages4
JournalScience
Volume199
Issue number4333
DOIs
StatePublished - Jan 1 1978

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Pancreatic Ribonuclease
Mercaptoethanol
Ribonucleases
Cyclic CMP
Cytidine
Sulfhydryl Compounds
Cations
Chromatography
Temperature
Enzymes

ASJC Scopus subject areas

  • General

Cite this

Enhancement of bovine pancreatic ribonuclease activity by mercaptoethanol. / Watkins, John B.; Benz, F. W.

In: Science, Vol. 199, No. 4333, 01.01.1978, p. 1084-1087.

Research output: Contribution to journalArticle

Watkins, John B. ; Benz, F. W. / Enhancement of bovine pancreatic ribonuclease activity by mercaptoethanol. In: Science. 1978 ; Vol. 199, No. 4333. pp. 1084-1087.
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