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. 1973 Feb;131(2):191–198. doi: 10.1042/bj1310191

Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties

Maria Giulia Battelli 1, E Lorenzoni 1, F Stirpe 1
PMCID: PMC1177458  PMID: 4352904

Abstract

1. The xanthine oxidase of cow's milk, crude or purified, appears as an oxidase (type O), and can be converted almost completely into a NAD+-dependent dehydrogenase (type D) by treatment with dithioerythritol or dihydrolipoic acid, but only to a small extent by other thiols. 2. The D form of the enzyme is inhibited by NADH, which competes with NAD+. 3. The kinetic constants of the two forms of the enzyme are similar to those of the corresponding forms of rat liver xanthine oxidase. 4. Milk xanthine oxidase is converted into an irreversible O form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin. 5. The enzyme as purified shows a major faster band and a minor slower band on gel electrophoresis. The slower band is greatly reinforced after xanthine oxidase is converted into the irreversible O form by chymotrypsin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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