Properties of aryl hydrocarbon hydroxylase in microsomes of Morris hepatoma 5123D and the host liver.

Properties of aryl hydrocarbon hydroxylase in the microsomes were compared between Morris hepatoma 5123D and the host liver from rats bearing this tumor. Requirement of NADPH for the assay of the enzyme activity was observed, compared to that of NADH, and also the additive effect of NADH on the requirement of NADPH was found in the tumor and liver. Curve of pH optimum of the enzyme activity in tumor and liver differed between the rats treated with corn oil and those with 3-methylcholanthrene, indicating a slight shift of the peak value to alkaline pH in the latter. The same values of the apparent Km for NADPH and NADH were shown for the enzyme from the liver and tumor even 24 hr after the treatment with 3-methylcholanthrene, but a difference in the apparent Km for benzo[a]pyrene was demonstrated between the tumor and the host liver, showing 3.6 approximately 6.6 muM in the former and 9.1 approximately 20 muM in the latter. By the addition of 7,8- or 5,6-benzoflavone to the assay medium for the tumor, the induced enzyme was inhibited noncompetitively, and the constitutive enzyme was enhanced, as demonstrated in the host liver. As observed in the induced enzyme in both tissues, cyclohexene oxide and 1,1,1-trichloropropane oxide slightly increased the activity of the constitutive enzyme in the tumor, in contrast to its inhibition in the host liver.