The blood of man is rich in plasminogen, the inactive precursor of plasmin, a protease (Astrup, 1956a); the most characteristic action of plasmin is the digestion of fibrin, i.e. fibrinolysis. Many tissues, including the prostate (Rasmussen and Albrechtsen, 1960a), contain substances which can activate plasminogen, and thus initiate fibrinolysis, and it has been assumed that both the excessive fibrinolysis seen in the blood of some patients with prostatic disease (Tagnon, Whitmore, Schulman and Kravitz, 1953a), and in prostatic surgery (Lombardo, 1957), is due to the release of this activator into the blood stream (Fearnley, 1965). Human semen contains a substance which can activate the blood fibrinolytic system (von Kaulla and Shettles, 1953). Indeed, when human seminal fluid is ejaculated, it undergoes a process resembling the clotting and fibrinolysis of the blood, by coagulating then liquefying spontaneously. The coagulum is formed when a fibrinogenlike protein secreted by the seminal vesicles is acted upon by a clotting enzyme from the prostate (Mann, 1964). Coagulation is followed within about 20 minutes by liquefactionliquefaction of the clots by an enzyme assumed to come from the prostate (Huggins and Neal, 1942). This enzyme resembles plasmin in that it is a protease acting on a fibrin-like substrate, and that it is derived from an
inactive precursor.
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uct/oai:localhost:11427/32014 |
| Date | 08 April 2020 |
| Creators | Kester, Ralph Charles |
| Contributors | Toadd, Alistair S |
| Publisher | Faculty of Health Sciences, Department of Surgery |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Type | Masters Thesis, Masters |
| Format | application/pdf |
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