Affiliation:
1. Department of Physiology and Pharmacology, Wayne State University College of Medicine, Detroit, Michigan
Abstract
Concentrates of platelet factor 1 were made from bovine platelets. Being bound to fine particles, the activity was not obtained in solution. The activity of the concentrates is destroyed by heating at 53 °C., at pH 5.2, by extraction with ether, by drying with acetone, or by standing at −20 °C. The concentrates accelerated the clotting of whole blood, and also the activation of prothrombin either to form thrombin or a non-thrombin derivative. Activation of purified prothrombin occurred under several different circumstances, and different end products formed. Platelet factor 1 concentrates appear to have a general property of accelerating alterations in the prothrombin molecule independently of these variants.
Publisher
Canadian Science Publishing