The inhibition of bovine xanthine oxidase activity by Hg2+ and other metal ions

The inhibition of the activity of bovine xanthine oxidase (XO) by divalent mercury and other metal ions has been investigated by optical spectroscopy and stop-flow kinetic measurements. The study shows that Hg2+ ion completely inhibits the activity of XO, while other metal ions such as Zn2+, Mg2+, C...

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Bibliographic Details
Published in:Journal of inorganic biochemistry 1996-06, Vol.62 (4), p.271-279
Main Authors: Mondal, M S, Mitra, S
Format: Article
Language:English
Subjects:
Animals
Cattle
Copper - pharmacology
Female
Kinetics
Mercury - pharmacology
Metals - pharmacology
Spectrophotometry - methods
Xanthine Oxidase - antagonists & inhibitors
Xanthine Oxidase - chemistry
Xanthine Oxidase - metabolism
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Summary:The inhibition of the activity of bovine xanthine oxidase (XO) by divalent mercury and other metal ions has been investigated by optical spectroscopy and stop-flow kinetic measurements. The study shows that Hg2+ ion completely inhibits the activity of XO, while other metal ions such as Zn2+, Mg2+, Co2+, and Ni2+ inhibit the activity only marginally (approximately 10%). The inhibition by the Hg2+ ion was found to be monophasic and noncompetitive with strong affinity for binding to XO. The pH-dependent study of the inhibition indicates that at least two ionizing groups of XO are involved in the binding of the Hg2+ ion.
ISSN:0162-0134
DOI:10.1016/0162-0134(95)00160-3