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• W2001893244 abstract "Two l-(+)-Lactate : cytochrome c oxidoreductases (EC 1.1.2.3) namely the S-flavocytochrome b2 and the H-flavocytochrome b2 were respectively extracted under the « crystallineform from the yeast Saccharomyces cerevisiae [7–9] and under the « pureform from the yeast Hansenula anomala [10]. At low ionic strength (10 mM phosphate buffer — pH 7.20), these two enzymes gave stable complexes with horse heart cytochrome c. From ultracentrifugation experiments on sucrose gradients, it can be concluded that the S-flavocytochrome b2, under its tetramer form, binds with only one molecule of cytochrome c. This molecular ratio remained invariant when modifying the centrifugation time. On the other hand, similar experiments carried out on H-flavocytochrome b2, under its tetramer form, lead to the conclusion that this enzyme binds with four molecules of cytochrome c. The same result was obtained by Sephadex gel chromatography. When prepared under the monomer form (low ionic strength, 1 h at 20°C), the H-flavocytochrome b2 binds with one molecule of cytochrome c. The protein associations are mainly due to electrostatic interactions since they proved to be ionic strength dependent. Moreover, the measured molecular ratios remained whether the cytochrome c was oxydized or reduced. The two different molecular ratios observed in the binding of cytochrome c to S or H-flavocytochrome b2 could be explained if considering that the « crystallineS-flavocytochrome b2 is not the physiological form of the enzyme. Les S et H-flavocytochrome b2 forment, à faible force ionique, un complexe stable avec le cytochrome c de cœur de cheval. Le S-flavocytochrome b2 fixe une seule molécule de cytochrome c par tétramère ; le H-flavocytochrome b2 accepte quatre molécules de cytochrome c par unité tétramérique. Les liaisons entrant en jeu lors de l'association entre ces deux molécules sont pour l'essentiel de type électrostatique, car très sensibles aux effets de force ionique ; de plus, le complexe n'est absolument pas dissocié par passage sur tamis moléculaire. L'état (oxydé ou réduit) du cytochrome c, ne modifie pas le rapport nombre de molécules de cytochrome c fixées par molécule de flavocytochrome b2." @default.
• W2001893244 created "2016-06-24" @default.
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• W2001893244 date "1977-10-01" @default.
• W2001893244 modified "2023-09-27" @default.
• W2001893244 title "Complexes entre les L (+) lactate : cytochrome c oxydoréductase extraite des levures Saccharomyces cerevisiae ou Hansenula anomala et le cytochrome c de cœur de cheval" @default.
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• W2001893244 doi "https://doi.org/10.1016/s0300-9084(77)80171-5" @default.
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