Enzymatic studies of the effect of Cu (II) on oxygen radical production stimulated by daunorubicin and ametantrone.
Daunorubicin can bind Cu (II) in Tris-HCl buffer (pH 7.4) and in the presence of NADH (100 microM). The complex is very stable. Cu (II) is not removed from the complex by cytochrome c reductase. The complexation of Cu (II) to daunorubicin gives rise to a modification of its redox properties. The complex, unlike the free drug, does not stimulate oxygen radical production. Ametantrone can also form a complex with Cu (II) in the conditions of enzymatic assays. Nevertheless, this complex is not stable in the presence of cytochrome c reductase. It dissociates immediately after the addition of the enzyme with releasing the metal ion.
Tarasiuk
J
J
Department of Pharmaceutical Technology and Biochemistry, Technical University, Gdansk, Poland.
Kolodziejczyk
P
P
Borowski
E
E
D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D003300:Copper; D003579:Cytochrome Reductases / Q000378:metabolism*; D003630:Daunorubicin / Q000494:pharmacology*; D005609:Free Radicals; D008942:Mitoxantrone / Q000031:analogs & derivatives* / Q000494:pharmacology; D009243:NAD / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism
D000970:Antineoplastic Agents; D005609:Free Radicals; D009243:NAD; D013481:Superoxides; D003300:Copper; D008942:Mitoxantrone; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase; C020182:ametantrone; D010100:Oxygen; D003630:Daunorubicin