Abstract
Summary
Fractionation of human semen on DEAE (diethylaminoethyl)-cellulose has shown that the seminal proteolytic activity at low pH is eluted as a single peak of proteolytic activity. This peak of proteolytic activity exhibits no milk clotting activity unless it is first activated by acidificaton. The chro-matographic mobilities of the proteolytic activity at low pH of unacidified and acidified semen are similar to those of unacidified and acidified gastric mucosal pepsinogen I, respectively. The possible conversion of seminal pepsinogen to pepsin by weakly acidic vaginal secretions posed the question of a possible role for pepsin in human reproduction.
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