VARIATIONS IN H-3 DIISOPROPYLFLUOROPHOSPHATE BINDING-PROTEINS IN HUMAN SEMINAL PLASMA

We have characterized the electrophoretic pattern and variations in H-3-diisopropylfluorophosphate (DFP)-binding proteins in human seminal plasma from normal men and from 103 patients attending the infertility clinic of our hospital. This study shows that 34 kDa prostate-specific antigen (PSA) is the major H-3-DFP-binding protein and that two other ubiquitous bands of 100 and 60 kDa are also present in seminal plasma from all the men studied. Additional bands of 92, 50-54 (doublet) and 38 kDa were also observed in some patients. The 38 kDa band was shown to be a highly glycosylated form of PSA. Further complexity was demonstrated by two-dimensional gel electrophoresis in the 27-30 kDa range of the gels since at least 10 major spots and rows of spots were seen. The concentration of these spots, including PSA, was extremely variable, as was their pattern of inhibition by various active site inhibitors of serine-proteases; these variations were not correlated with any specific sperm characteristics. With the exception of PSA, the proteins have not been identified. Their distribution suggests that most of them are exclusively of prostatic origin although a few could also derive from the seminal vesicles or blood. Future studies will be aimed at determining the nature of these proteins and their potential usefulness in andrology.