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The preceding paper of this series (1) reports on the presence in yeast of an enzyme system catalyzing the reduction of the sulfate of 3'-phosphoadenosine-5'-phosphosulfate to sulfite.It was observed that 3 nondialyzable fractions, two of them heatlabile (Enzymes A and B) and one heat-stable (Fraction C), were required for the reaction.Furthermore, incubation of two of the fractions, Enzyme A and Fraction C, with reduced triphosphopyridine nucleotide led to the appearance of -SH.This reaction has been tentatively formulated as follows:Fraction C-SS + TPNH + H+ Enzyme A 0)Fraction C(SH)s + TPNThe purification and properties of Enzyme A are described in this paper.It is shown that Enzyme A is relatively specific for the reduction of a disulfide group of Fraction C. The system Enzyme A plus Fraction C, however, will reduce other disulfides such as 5,5'-dithiobis(2-nitrobenzoic acid) or lipoamide.
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Asahi et al. (1961) studied this question.
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