Xanthine oxidase and milk flavoprotein

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Abstract
A method was descr. for preparing a , flavoprotein which catalyzed the oxidation of hypoxanthine, aldehydes and dihydrocoenzyme 1, and was ca. 1000 times more active per mg. dry wt. than milk. The 3 catalytic activities although associated with the same flavoprotein were differentially inactivated. Drying and incubation with cyanide abolished hypoxanthine-aldehyde activity without affecting either dihydrocoenzyme-l activity or the snectrum and chemical properties of the flavoprotein. The flavin moiety was shown to be very similar to, if not identical with, flavinadenine dinucleotide. Flavin accounted for only 35% of the total absorption at 450 m[mu]. Evidence was presented for the existence of a non-flavin colored group in the molecule. The catalytic role of this additional group was not as yet clarified. No direct evidence was obtained that the flavin groups underwent a cycle first of reduction by the 3 substrates and then of oxidation by some oxidizing agents.

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