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- W2010998047 abstract "The difference spectrum of oxidized enzyme minus d-lactate-reduced enzyme reveals the characteristic absorption bands of an oxidized flavin bound to the protein. The wavelengths of the peaks are: 455 mμ and 385 mμ. The oxidation-reduction potential of the FAD bound to the d-lactate dehydrogenase (d-2-hydroxyacid: (acceptor) oxydoreductase) of anaerobic yeast has been determined. A spectrophotometric study of the equilibrium between the flavin group and the d-lactate-pyruvate system gives values of EmF = −0.178 Volt at pH7.0 and 30°. The pH-dependence coefficient of this potential is ΔEmF/ΔpH = −0.03 V. Le potentiel d'oxydoréduction de la d-lacticodéshydrogénase (d-2-hydroxyacide: (accepteur) oxydoréductase) de la levure anaérobie a été déterminé spectrophotométriquement par l'étude de l'équilibre entre l'enzyme et le système d-lactate-pyruvate. La valeur obtenue pour Em à pH 7.0 et à 30° est de −0.178 V avec la pente ΔEm/ΔpH −0.03 V par unité de pH. Le spectre différentiel de la d-LDH oxydée par rapport à la d-LDH réduite par le d-lactate, montre deux pics caractéristiques de la flavine, l'un à 455 mμ, l'autre à 385 mμ." @default.
- W2010998047 created "2016-06-24" @default.
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- W2010998047 date "1963-01-01" @default.
- W2010998047 modified "2023-10-01" @default.
- W2010998047 title "Potentiel d'oxydoréduction de la d-2-hydroxyacide: (accepteur) oxydoréductase de la levure anaérobie" @default.
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- W2010998047 doi "https://doi.org/10.1016/0006-3002(63)90542-0" @default.
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