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ANALGESICS AND ENZYMES OF THE CYTOCHROME CHAIN

1953; American Society for Pharmacology and Experimental Therapeutics; Volume: 108; Issue: 3 Linguagem: Inglês

10.1016/s0022-3565(25)05210-3

1521-0103

R.I.H. Wang, James A. Bain,

Enzyme Catalysis and Immobilization

Direct assay of enzyme activities by spectrophotometric methods demonstrated that DPN-cytochrome c reductase was the most sensitive of the cytochrome chain enzymes to the inhibitory action of morphine. In addition to the above inhibition, morphine and its derivatives having a free phenolic hydroxyl were shown to be active in catalyzing the transfer of electrons from reduced DPN to ferricytochrome c in the absence of enzyme. Potency as transferring agents was shown to be correlated with potency as inhibitors of DPN-cytochrome c reductase. Methadone had the most striking effect on cytochrome c oxidase stimulating at low concentrations and inhibiting at high concentrations. The l-isomer was more potent than the d-isomer. Meperidine apparently was most effective as an inhibitor of the dehydrogenase step in the malic dehydrogenase-DPN-cytochrome c reductase system having only a relatively small effect on cytochrome c oxidase.