A new irreversibly inhibited form of xanthine oxidase from ethylisonitrile

The treatment of xanthine oxidase with ethylisonitrile results in irreversible inhibition of the catalytic activity. Chemical and spectroscopic evidence suggests that the inhibited enzyme is a new distinct derivative in which the essential sulfido ligand to molybdenum has been modified or removed.

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Bibliographische Detailangaben
Veröffentlicht in:	Journal of inorganic biochemistry 1997-04, Vol.66 (1), p.63-65
Hauptverfasser:	Holmer, Shelley A, Houlton, Cynthia L, David Westmoreland, T
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Cattle Electron Spin Resonance Spectroscopy In Vitro Techniques Kinetics Ligands Molecular Structure Molybdenum - chemistry Nitriles - pharmacology Sulfides - chemistry Xanthine Oxidase - antagonists & inhibitors
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Beschreibung
Zusammenfassung:	The treatment of xanthine oxidase with ethylisonitrile results in irreversible inhibition of the catalytic activity. Chemical and spectroscopic evidence suggests that the inhibited enzyme is a new distinct derivative in which the essential sulfido ligand to molybdenum has been modified or removed.
ISSN:	0162-0134 1873-3344
DOI:	10.1016/S0162-0134(96)00185-7