Purification of rat epididymal proteins `D‘ and `E’, demonstration of shared immunological determinants, and identification of regional synthesis and secretion

Abstract

Two acidic secretory epididymal glycoproteins, protein D of 27,000 daltons and protein E of 28,000 daltons, were purified and antisera prepared against each separately. Both proteins shared common immunological determinants when tested by double immunodiffusion and tandem crossed immunoelectrophoresis. By selective immunoprecipitation, protein D was synthesized and secreted by all regions of the epididymis with the exception of the initial segments. In contrast, the synthesis and secretion of protein E was restricted to the corpus and proximal cauda.