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Purification of an NADH-(dichlorophenol-indophenol) oxidoreductase from Bacillus stearothermophilus.

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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