Mondal, Madhu Sudan ; Mitra, Samaresh (1996) The inhibition of bovine xanthine oxidase activity by Hg2+ and other metal ions Journal of Inorganic Biochemistry, 62 (4). pp. 271-279. ISSN 0162-0134
Full text not available from this repository.
Official URL: http://linkinghub.elsevier.com/retrieve/pii/016201...
Related URL: http://dx.doi.org/10.1016/0162-0134(95)00160-3
Abstract
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 (~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.
Item Type: | Article |
---|---|
Source: | Copyright of this article belongs to Elsevier Science. |
ID Code: | 20088 |
Deposited On: | 20 Nov 2010 15:02 |
Last Modified: | 03 Mar 2011 08:11 |
Repository Staff Only: item control page