A method is presented for 160hydroxylase (SAH) induction in cultured human lymphocytes. SAH, a microsomal-associated enzyme, effects the oxidative conversion of 17pestradiol to estriol, which competes for cytoplasmic binding sites. 17,-estradiol and estrone are known mammary carcinogens, while estriol and its epimers have been suggested to have anticarcinogenic properties. To substantiate genetic variations of hydroxylase activity, an analysis of estrogen-induced cultured human lymphocytes was conducted to evaluate the frequency distribution of low, intermediate, and high SAH activity. Frequency analysis indicated that the control population distribution of SAH activity does not corroborate a proposed trimodal expansion of human SAH activity. A log normal distribution of SAH activity does exist, which suggests a polygenic mode of genetic control. SAH activity in a population of breast cancer patients and relatives of breast cancer patients showed no statistical difference from the SAH activity in the control population.

Cultured human lymphocytes may be assayed for aryl hydrocarbon hydroxylase (AHH) in whole cell preparations. The optimum assay conditions are pH 8.5, and 1.5 mM Mg++. The reaction is linear with time and cell number, and is inhibited by CO. Estradiol may inhibit induction of AHH by 3-methylcholanthrene, but is a poor competitor for the enzyme. A Caucasian population was assayed for AHH activity. The distribution was lognormal; no difference was found in cultured cells from males and females or smokers and nonsmokers. Cells from relatives of lung cancer patients showed higher activity. An American Indian population showed no difference from the Caucasian population in enzyme level. No linkage was found between AHH and 16a-hydroxylase.