Lack of competition between cytochrome c and anthraquinone type drugs for the reductive sites of NADH dehydrogenase.
We have shown that (i) the cytochrome c reductase activity of the commercial NADH dehydrogenase does not perturb its ability to catalyse the reduction of various antitumor compounds of the anthracycline class, (ii) the reduction of these compounds by NADH, catalysed by commercial NADH dehydrogenase, correlates with their reduction by NADH catalysed by microsomes. Moreover, our data strongly suggest that two catalytic sites are present, one for cytochrome c and one for quinone type compounds.
Tarasiuk
J
J
Department of Pharmaceutical Technology and Biochemistry, Technical University of Gdansk, Poland.
Garnier-Suillerot
A
A
Borowski
E
E
D000818:Animals; D000880:Anthraquinones / Q000378:metabolism*; D000970:Antineoplastic Agents / Q000378:metabolism*; D001667:Binding, Competitive; D003579:Cytochrome Reductases / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D008862:Microsomes, Liver / Q000378:metabolism; D009243:NAD / Q000378:metabolism*; D009245:NADH Dehydrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains
D000880:Anthraquinones; D000970:Antineoplastic Agents; D003574:Cytochrome c Group; D009243:NAD; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase