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. 1974 Nov;143(2):465–468. doi: 10.1042/bj1430465

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites (Short Communication)

William F Cleere 1, Carmel O'Regan 1, Michael P Coughlan 1
PMCID: PMC1168404  PMID: 4462563

Abstract

Turkey liver xanthine dehydrogenase containing the full complement of molybdenum, flavin and iron–sulphur prosthetic groups is, as normally isolated, a mixture of functional and non-functional enzyme. The latter apparently lacks the cyanolysable persulphide groups essential to the oxidation of xanthine and to interaction with arsenite. These groups are not required for the oxidation of NADH by Methylene Blue. That KI treatment effects a differential release of flavin from xanthine-prereduced and NADH-prereduced enzyme merely reflects the degree of functionality of the preparations used and may not be taken as evidence for non-equivalence of the flavin chromophores.

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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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