Prothrombin activation by a metalloprotease from Staphylococcus aureus

Abstract
Formation of thrombin during incubation of purified bovine prothrombin with purified staphylococcal metalloprotease was investigated. Thrombin activity was estimated by examination of clotting time and by digestion of a synthetic substrate, Chromozym TH. The metalloprotease caused direct activation of prothrombin which was inhibited by the addition of EDTA. Metalloprotease produced by some strains of S. aureus may simulate staphylocoagulase activity.