Two-dimensional electrophoresis of proteins in various fractions of the human split ejaculate.

Two-dimensional electrophoresis of six fractions of split ejaculates from normal men (median age 23 years, n = 6) revealed large differences in the pattern of proteins found between the prostate-enriched fractions and secretions associated with the seminal vesicles. The glandular contributions were assessed using the concentrations of spermine, zinc and prostatic acid phosphatase (PAP) for prostatic secretion, and fructose and prostaglandin E for seminal vesicle secretion in the various fractions. Aside from PAP, four additional proteins were apparently associated with the prostatic fraction, one of which shared the biochemical characteristics of the specific ventral lobe protein of the rat prostate, prostatein (molecular mass 16000, pI 4.8). The presumptive vesicular fractions contained a large number of low molecular mass proteins (10–20 000), with widely varying pI-values. The concentration of albumin and transferrin appeared to be highest in the sperm cell enriched fractions, indicating a major contribution to the ejaculate of testicular epididymal origin.