Ação de Sais de Cobre sobre a Xantina Desidrogenase na Carcinogênese Hepática de Ratas
DOI:
https://doi.org/10.32635/2176-9745.RBC.1984v30n4.3465Keywords:
Xanthine Dehydrogenase, CarcinogenesisAbstract
Blood serum xanthine dehydrogenase activity was inhibited by cupric acetate (CuAc) (12,5 mg/100 g body weight). The study of the inhibition by CuAc was related with the hepatic changes produced by D-L-ethionine (12,5 mg/100 g body weight). "In vitro" experiments showed that CuAc is a potent inhibitor of the xanthine dehydrogenase activity and that this inhibition is of a non-competitive type. Ehtionine protects against the inhibitory effect of CuAc, both "m vivo" as "in vitro", probably by the formation of a copper complex. Experiments with O2 as eléctron acceptor seemed to indicate that the cupric sait competes "m vitro" with the reduction of the triphenyltetrazolium chloride in the electron transfer reaction.
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