A new irreversibly inhibited form of xanthine oxidase from ethylisonitrile
| Autor: | Shelley A Holmer, T. David Westmoreland, Cynthia L Houlton |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Xanthine Oxidase
Stereochemistry chemistry.chemical_element In Vitro Techniques Sulfides Ligands Biochemistry Catalysis Inorganic Chemistry chemistry.chemical_compound Nitriles Animals Xanthine oxidase Molybdenum chemistry.chemical_classification Binding Sites Molecular Structure Ethylisonitrile Electron Spin Resonance Spectroscopy Ligand (biochemistry) Kinetics Enzyme Xanthine dehydrogenase chemistry Cattle Derivative (chemistry) |
| Zdroj: | Journal of Inorganic Biochemistry. 66:63-65 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/s0162-0134(96)00185-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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