Induced protein is a commonly measured marker for estrogenic action. The induction of induced protein by o,p'-DDT was studied in an in vitro system. Nuclear levels of estrogen receptor translocated by o,p'-DDT correlated highly with induced protein induction, and the time course for induced protein induction was consistent with an estrogen receptor-mediated mechanism. While the maximum amount of induced protein produced by o,p'-DDT was less than after 17 beta-estradiol exposure, the induced protein formed by each compound was indistinguishable on nondenaturing and denaturing polyacrylamide gels. Also, it was shown that o,p'-DDT does not cause additional induction of induced protein over that seen with maximum levels of 17 beta-estradiol, further supporting the premise that these compounds share a common pathway in stimulating the synthesis of induced protein.