Abstract
Electrophoresis of semen on cellulose acetate strips allowed the localization of 19 protein bands. Twelve of these were analyzed for their composition and ten for their tissue of origin. Four bands were composed of prostatic products, three contained secretions form the seminal vesicles, and various serum products composed six others. Assays were also performed for acid phosphatase activity, glycoproteins and proteins bound to zinc. Proteins in semen were found to be broken down with time during incubation at 37C and therefore only fresh specimens or material which is frozen immediately after liquefaction may be used with these techniques. Our experiments clearly show that electrophoresis of semen may be a useful technique in clinical andrology: in particular in the case of excretory azoospermia and infections of the genital tract.
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