Posttesticular surface modifications and contributions of reproductive tract fluids to the surface polypeptide composition of boar spermatozoa.

Caput and cauda epididymal fluids were found to be exceedingly rich in the numbers and kinds of polypeptides when analyzed by two-dimensional (2-D) gel electrophoresis. Only a few of the major (Coomassie-stained) and minor (silver-stained) epididymal fluid polypeptides were identified on epididymal sperm plasma membranes (PM) and even fewer identified in ejaculated sperm. The 2-D electrophoretic patterns of caput sperm PM differed little from those of cauda sperm PM. Thus, epididymal transit resulted in relatively minor quantitative and qualitative modifications in sperm PM composition. Seminal plasma showed a few major polypeptides from the cauda epididymal fluid, but the major constituents were those polypeptides from the seminal vesicle secretions. Sperm appear to acquire one acidic high molecular weight polypeptide from either the bulbourethral gland or prostate gland, and another major acidic polypeptide of high molecular weight from the seminal vesicle gland. Numerous neutral and basic low molecular weight polypeptides, originating from the seminal vesicles, adhered tightly to sperm. These were major polypeptides and constituted a substantial percentage of the total PM protein. Thus, major contributions to the sperm PM polypeptide profile occurred at ejaculation. This study did not address loosely bound polypeptides but is the first to analyze, in a comprehensive way, the origins of tightly bound sperm polypeptides from a single species.