ABP, a Sertoli cell secretory product, was identified in the seasonal rodent Octodon degus (Molina, 1872). It was shown to be present in cytosols from the testis and epididymis. It migrated with an Rf of 0.37 on nondenaturing polyacrylamide gels. Ligation of the vas efferens caused the disappearance of ABP from the epididymis and its accumulation in the testis, indicating its testicular origin. Binding to [3H]5 alpha-DHT was specific and completely reversible, with an apparent Kd of 3.5 +/- 0.4 X 10(-9) M. Half-times of association and dissociation were at 15 and 120 minutes, respectively. Binding equilibrium was achieved at 120 minutes. Steroid affinity relative to the best competitor, 5 alpha-DHT, was 0.27 for testosterone, 0.06 for 17 beta-estradiol, and 0.01 for cyproterone acetate. The presence and similar characteristics of ABP in a wide variety of mammals, including those with special reproductive strategies such as seasonal breeding, suggests that this protein may play a general role in the mechanisms regulating spermatogenesis, probably affecting the transport and concentration of androgens in the testis and epididymis.