Purification, kinetic behavior, and regulation of NAD(P)+ malic enzyme of tumor mitochondria

The purification and kinetic characterization of an NAD(P)+-malic enzyme from 22aH mouse hepatoma mitochondria are described. The enzyme was purified 328-fold with a final yield of 51% and specific activity of 38.1 units/mg of protein by employing DEAE-cellulose chromatography and an ATP affinity co...

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Veröffentlicht in:The Journal of biological chemistry 1984-05, Vol.259 (10), p.6222-6227
Hauptverfasser: Moreadith, R W, Lehninger, A L
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Sprache:eng
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