Electrophoretic characterization of mouse epididymal esterases in inbred lines and in a natural population

Esterase isozymes were studied in mouse epididymis of two inbred strains (C57BL, DBA/2) and in a natural population (Swiss OF1), by using vertical polyacrylamide gel electrophoresis and staining with alpha or beta-naphthyl acetate as a substrate. Eighteen (C57BL), 17 (DBA/2) or 16 (Swiss OF1) epididymal isozymes were separated; four were common to the testis, and five to both the testis and the serum. The use of different inhibitors showed that carboxylesterase activities account for the greater part of the total epididymis non-specific esterase activity. This comparative study revealed minor interspecies variations since only two isozymes were not expressed in the same manner in the three populations examined. Among the nine isozymes which appeared solely in the epididymis, the profiles varied between tissues and fluids as well as between the proximal part in which sperm maturation occurs and the distal part where sperm storage takes place. The variations proceeded from the relative activity of isozymes and the presence or absence of some of them; two characterized the proximal part and one the distal part in the three species. By comparing testis and epididymal tissues and fluids, it is suggested that the isozymes found in epididymal fluids originated from the testis, the epididymal epithelium or both. In addition to this epididymal secretory function, the lack in the fluid of the distal part of one isozyme identified in the testis, and two in the proximal part may also provide evidence for its reabsorptive function.