INVESTIGATION OF THE MECHANISM OF FIBRINOLYSIS
Annual progress rept. 1 Jul 1962-30 Jun 1963,
APPLIED BIOLOGICAL SCIENCES LAB INC GLENDALE CA
Pagination or Media Count:
In in vitro studies bovine pancreatic ribonuclease has been found to inhibit the depolymerization and hydrolysis of bovine fibrin by plasmin of human origin. The human plasmin utilized was observed to enhance the nuclease enzyme activity of bovine pancreatic ribonuclease. Studies made on the role of heparin and ribonuclease in fibrinolysis have indicated that heparin inhibits the antiplasmin activity of ribonuclease. In addition, it has been found that heparin in low con centration 1 - 10 NIH units induces liquefaction of fibrin clots in vitro without added plasmin. Bovine pancreatic ribonuclease will inhibit this effect of heparin. Dilute acid hydrolysis of bovine pancreatic ribonuclease 0.01N - 0.075N hydrochloric acid results in the loss of the nuclease activity of ribonuclease but not the antiplasmin activity of ribonuclease. The data obtained are discussed in terms of the mechanism of fibrinolysis and the functions of ribonuclease and heparin.
- Anatomy and Physiology