Purification and characterization of androgen binding protein from rabbit epididymis.

A method for the purification of androgen binding protein (ABP) from the rabbit epididymis is presented. Epididymal extracts were submitted to sequential ammonium sulfate precipitation, androgen affinity chromatography, concanavalin A (Con A) affinity chromatography, and preparative polyacrylamide gel electrophoresis. Since the blood protein testosterone-estradiol binding globulin (TeBG) was a possible component of the epididymal extract, ABP was differentiated and separated from TeBG by affinity chromatography on Con A-Sepharose since the latter protein was shown to be completely absorbed by the lectin while the former was not. The final product was shown to be pure by polyacrylamide gel electrophoresis. Electrophoresis in the presence of sodium dodecyl sulfate revealed that ABP is comprised of subunits.