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. 1967 Nov;105(2):585–589. doi: 10.1042/bj1050585

Xanthine oxidase inactivation by reagents that modify thiol groups

R C Green 1, P J O'Brien 1
PMCID: PMC1198348  PMID: 5626093

Abstract

1. The presence of xanthine was required for the inhibition of bovine milk xanthine oxidase by o-iodosobenzoate, iodoacetamide, hydrogen peroxide or p-chloromercuribenzoate. 2. Inactivation by p-chloromercuribenzoate was very rapid, was reversed by cysteine and was less in the presence of FAD. Lineweaver–Burk plots showed that the inactivation by p-chloromercuribenzoate was competitive with substrate. 3. Inactivation by o-iodosobenzoate, iodoacetamide or hydrogen peroxide could not be reversed by cysteine or xanthine. However, the presence of xanthine during the incubation with inhibitor protected the enzyme against o-iodosobenzoate but not against iodoacetamide or hydrogen peroxide. 4. p-Chloromercuribenzoate protected the enzyme against inactivation by hydrogen peroxide.

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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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