Selective Inhibition of Fe- versus Cu/Zn-Superoxide Dismutases by 2,3-Dihydroxybenzoic Acid Derivatives
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概要
- 論文の詳細を見る
A series of catechol derivatives were synthesised and tested for their ability to inactivate the iron-containing superoxide dismutase (Fe-SOD) from Escherichia coil and the bovine erythrocytes Cu/Zn-SOD. Incubation of catechols with Fe- or Cu/Zn SODs resulted in a time-dependent loss of enzyme activity with highly selective inhibition for the iron-dependent enzyme. Catechol-induced inactivation of SODs was correlated with the auto-oxi-dation of the catechol compounds to their corresponding ortho-quinone derivatives, which was found to be non-dependent on the presence of enzymes. Mass electrospray experiments on catechol-incubated Fe-SOD provided evidence for the irreversible nature of the inhibition process, yielding to a complex mixture of modified proteins.
- 公益社団法人日本薬学会の論文
- 2002-05-01
著者
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Hoffmann P
Groupe De Chimie Organique Biologique Laboratoire De Synthese Et Physico-chimie De Molecules D'
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Viode Cecile
Groupe De Chimie Organique Biologique Laboratoire De Synthese Et Physico-chimie De Molecules D'
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SOULERE Laurent
Groupe de Chimie Organique Biologique, Laboratoire de Synthese et Physico-Chimie de Molecules d'Inte
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PERIE Jacques
Groupe de Chimie Organique Biologique, Laboratoire de Synthese et Physico-Chimie de Molecules d'Inte
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HOFFMANN Pascal
Groupe de Chimie Organique Biologique, Laboratoire de Synthese et Physico-Chimie de Molecules d'Inte
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Soulere Laurent
Groupe De Chimie Organique Biologique Laboratoire De Synthese Et Physico-chimie De Molecules D'
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Perie Jacques
Groupe De Chimie Organique Biologique Laboratoire De Synthese Et Physico-chimie De Molecules D'
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HOFFMANN Pascal
Groupe de Chimie Organique Biologique, Laboratoire de Synthese et Physico-Chimie de Molecules d'Interet Biologique; UMR-CNRS 5068-Universite Paul Sabatier