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. 1980 Nov 1;191(2):457–465. doi: 10.1042/bj1910457

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

I Mains, D M Power, E W Thomas, J A Buswell
PMCID: PMC1162236  PMID: 7236205

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.

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Selected References

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