Inhibition of camel lens ζ-crystallin/NADPH:Quinone oxidoreductase activity by chloranilic acid
| Autor: | Ali S. Duhaiman, Riskuwa A. Shehu, Abdulaziz A. A. Al‐Hamidi |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Camelus Chloranil Stereochemistry Clinical Biochemistry Electron donor Cell Biology Electron acceptor NAD(P)H Dehydrogenase (Quinone) Crystallins Biochemistry Benzoquinone Kinetics chemistry.chemical_compound chemistry Chloranilic acid Crystallin Benzoquinones Genetics Animals Molecular Biology IC50 |
| Zdroj: | IUBMB Life. 41:415-421 |
| ISSN: | 1521-6543 |
| DOI: | 10.1080/15216549700201431 |
| Popis: | Camel lens zeta-crystallin/NADPH:quinone oxidoreductase activity was inhibited by chloranilic acid (2,5-dichloro-3,6-dihydroxy-1,4-benzoquinone) with NADPH as an electron donor and 9,10-phenanthrenequinone (PQ) as an electron acceptor in a time-independent but concentration dependent manner. The IC50 of chloranilic acid was 1 microM. The inhibition was noncompetitive with respect to both NADPH and PQ as deduced by Lineweaver-Burk plots. The estimated inhibition constant (Ki) was 0.8 microM for both NADPH and PQ. Examination of other benzoquinones suggested that the presence of -OH and -Cl on benzoquinone was essential for the inhibition. |
| Databáze: | OpenAIRE |
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