An enzyme obtained from Bacillus cereus T spores which catalyzes the reduction of the disulfide, 5, 5′-dithiobis (2-nitrobenzoic acid) (DTNB), has been partially purified and characterized. The enzyme required either reduced nicotinamide adenine dinucleotide phosphate (NADPH 2 ) or reduced nicotinamide adenine dinucleotide (NADH 2 ) as electron donor. It had a pH optimum of 8, was destroyed by heating at 70C for 5 min, and was stimulated by Ca 2+ and Mg 2+ . No other small molecular weight disulfides were found to be substrates for the enzyme.
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Blankenship et al. (1971) studied this question.
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