Purification of an NADH-(dichlorophenol-indophenol) oxidoreductase from Bacillus stearothermophilus.
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ABSTRACT: An NADH-(dichlorophenol-indophenol) oxidoreductase was purified 104-fold and in 25% overall yield from the thermophilic bacterium Bacillus stearothermophilus, strain PH24. After solubilization in 2M-NaCl at 70 degrees C, the enzyme was purified by ion-exchange and hydroxyapatite chromatography, followed by affinity chromatography on immobilized Cibacron Blue 3GA. The purified enzyme had a mol.wt. of 43 000 and had an absorption spectrum characteristic of flavoprotein. The enzyme activity was enhanced by FMN and by CN-. The enzyme was inhibited by EDTA and by rho-chloromercuribenzoic acid.
SUBMITTER: Mains I
PROVIDER: S-EPMC1162236 | biostudies-other | 1980 Nov
REPOSITORIES: biostudies-other
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