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Molecular Pharmacology, Vol 19, 184-186, Copyright © 1981 by the American Society for Pharmacology and Experimental Therapeutics
1 Laboratory of Clinical Biochemistry, Baltimore Cancer Research Program, Division of Cancer Treatment, National Cancer
Institute, Baltimore, Maryland 21201
Several flavoenzymes are compared for their ability to catalyze reductive glycosidic cleavage of anthracycline antibiotics and to promote oxygen consumption in the presence of the antibiotics. NADPH cytochrome P-450 reductase, xanthine oxidase, nitrate reductase, NADH cytochrome c reductase, and lipoamide dehydrogenase catalyzed with decreasing specific activity the reductive glycosidic cleavage of daunorubicin and showed enhanced oxygen consumption in the presence of daunorubicin. Gluthione reductases, L-amino acid oxidase, D-amino acid oxidase, D-glucose oxidase, and lactic dehydrogenase were inactive. All of those flavoenzymes which catalyze reductive glycosidic cleavage possess single-electron transfer systems.
Note:
ACKNOWLEDGMENT
We wish to thank Ms. Helen Chlewicki in the preparation of the
manuscript.
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