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These results essentially rule out substitution at either 0 or N-1 of the guanine residue, since in such products enolization of the keto oxygen at C-6 of guanine wo~ld n~~ be possible. Reaction of 1'-acetoxyestragole wit~ [~ 4 H,B- C]deoxyguanosine yielded Adducts I, II, and III \'lith H: C ratios that were very similar to those of the deoxyguanosine used for the reactions. Thus, substitution at both N-7 and C-8 of the deoxyguan- E. MILLER AND J. MILLER 12 4000 ®MOUSE-LIVER DNA HYDROLYSATE E a.

Kinetic studies have shown that whereas 9hydroxyellipticine has lillie or no effect on the interaction of type I or type II substrates with cytochrome P-450, it exhibits marked noncompetitive inhibition of the interaction of type II substrates with cytochrome P-448. 9-Hydroxyellipticine administered to rats has also been shown to inhibit cytochrome P-448 activity, but not cytochrome P-450 activity, determined in vitro, and results in a 90% inhibition of ethoxyresorufin de-ethylase, a sensitive marker enzyme for cytochrome P448 activity (Delaforge, et al, 1980c).

Chasseaud, L. , 1979, The role of glutathione and glutathione ~-transferases in the metabolism of chemical carcinogens and other electrophilic agents, Adv. , 29:175. , and Maume, B. , 1978, Possible occurrence of the epoxide-diol metabolic pathway for hepatocarcinogenic safrole in cultured rat liver cells, as compared with whole animal: A metabolic study 18 E. MILLER AND J. MILLER by mass spectrometry, in: "Nass Spectrometry in Biochemistry and Medicine," A. Frigerio and N. , Spectrum Publications, New York.

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