[Skip to Content]
[Skip to Content Landing]
August 21, 1943

Current Comment

JAMA. 1943;122(17):1188-1189. doi:10.1001/jama.1943.02840340036015

SEMINAL FIBRINOLYSIN  Discovery of a proteolytic enzyme in human semen practically identical with the fibrinolysin secreted by virulent strains of hemolytic streptococci has been reported by Huggins1 of the Department of Surgery, University of Chicago. Human, guinea pig and canine semens are delivered in a liquid state, after which human and guinea pig semens coagulate to form an elastic solid, while canine semen remains fluid. Coagulated guinea pig semen remains in a solid state in the vagina for several days. Solidified human semen is spontaneously liquefied in a few minutes. Seminal coagulation is believed to be due to fibrinogen and thromboplastin2 derived from a special region of the prostate.3 Liquefaction of the resulting coagulum is apparently due to the combined action of two enzymes, a fibrinolysin and a "fibrinogenase." "Fibrinogenase" is dominant in canine semen, thus preventing coagulation, while fibrinolysin is dominant in human semen, lysis taking