Thrombosis and Haemostasis, Inhaltsverzeichnis Thromb Haemost 1959; 3(04): 548-553DOI: 10.1055/s-0038-1654409 Originalarbeiten — Original Articles — Travaux Originaux Schattauer GmbH Hydrolysis of Tosylarginine Methyl Ester by Russell’s Viper Venom Robert H. Wagner * 1 Department of Pathology, University of North Carolina, Chapel Hill, North Carolina USA , Robert A. Farrell * 1 Department of Pathology, University of North Carolina, Chapel Hill, North Carolina USA › Institutsangaben Artikel empfehlen Abstract Volltext als PDF herunterladen Referenzen References 1 Neurath H, Schwert G. W. The Mode of Action of the Crystalline Pancreatic Proteolytic Enzymes. Chem. Rev 1950; 46: 69 2 Deutsch E, Frischauf H. Untersuchungen über die Wirkung des Trypsins auf die Blutgerinnung. Acta haemat. (Basel 1955; 13: 161 3 Travis B. L, Ferguson J. H. Proteolytic Enzymes and Platelets in Relation to Blood Coagulation. J. clin. Invest 1951; 30: 112 4 Irving Jr. G. W, FrutOn J. S, Bergmann M. The Action of Intracellular Proteinases. J. biol. Chem 1941; 139: 569 5 Eagle H. J, Harris T. Studies in Blood Coagulation V. The Coagulation of Blood by Proteolytic Enzymes (Trypsin and Papain). J. gen. Physiol 20: 543 1936; 6 Bergmann M, Fruton J. S, Pollock H. The Specificity of Trypsin. J. biol. Chem 1939; 127: 643 7 Eagle H. J. Recent Advances in the Blood Coagulation Problem. Medicine (Baltimore 1937; 16: 95 8 Deutsch H. F, Diniz C. R. Some Proteolytic Activities of Snake Venoms. Venoms (Buckley and Porges, Eds.) American Association for the Advancement of Science; Washington, D. C: 1956: p. 199 9 Sherry S, Troll W. The Action of Thrombin on Synthetic Substrates. J. biol Chem 1954; 208: 95 10 Langdell R. D, Wagner R. H, Brinkhous K. M. Estimation of Antihemophilic Activity by the Partial Thromboplastin Time Technic. The Coagulation of Blood Tocantins L. M. Ed. Grune and Stratton; New York: 1955: p. 72 11 Patton T. B, Ware A. G, Seegers W. H. Clotting of Plasma and Siliconed Surfaces. Bloo 1948; 3: 656 12 Lineweaver H, Burk D. The Determination of Enzyme Dissociation Constants. J. Amer. chem. Soc 56: 658 1934;
