Thrombosis and Haemostasis, Table of Contents Thromb Haemost 1968; 19(03/04): 492-498DOI: 10.1055/s-0038-1651228 Originalarbeiten – Original Articles – Travaux Originaux Schattauer GmbH Activity-pH Relationship and Michaelis Constants during Activation of Profibrinolysin and during Fibrinogenolysis Authors Author Affiliations L. B Nanninga 1 Department of Physiology, University of Texas Medical Branch, Galveston, Texas M. M Guest * 1 Department of Physiology, University of Texas Medical Branch, Galveston, Texas Recommend Article Abstract Buy Article(opens in new window) Summary The pH dependence was investigated separately for the activation of Profibrinolysin by urokinase and for the breakdown of fibrinogen by fibrinolysin. The effects of concentration of the substrates, Profibrinolysin and fibrinogen, respectively, were investigated and Michaelis constants were estimated for both enzymatic reactions. The average concentration of Profibrinolysin in normal human plasma was found to be 1.4 × 10–6 M based on experiments with relatively pure Profibrinolysin. Full Text References References 1 Nanninga L.B. Rapid determination of Profibrinolysin (plasminogen) in plasma.. Thrombos. Diathes. haemorrh. (Stuttgart) 1967; 17: 8 2 Ware A.O, Guest M.M, Seegers W.H. Fibrinogen: with special reference to its preparation and certain properties of the product.. Arch. Biochem 1947; 13: 231 3 Nanninga L.B, Guest M.M. Antifibrinolytic action of the anticoagulant split product of fibrinogen.. Thrombos. Diathes. haemorrh. (Stuttg.) 1968; 19: 526 4 Bobbins K.C, Summaria L, Hsieh B, Shah R.J. The peptide chains of human plasmin.. J. biol. Chem 1967; 242: 2333 5 Nanninga L.B, Guest M.M. Rapid determination of antifibrinolysin (antiplasmin) in plasma.. Thrombos. Diathes. haemorrh. (Stuttgart) 1966; 15: 273 6 West E.S, Todd W.R. Textbook of Biochemistry.. Third ed.. McMillan Company; N.Y.: 1961: p. 407 7 Alkjaersig N, Fletcher A.P, Sherry S. The activation of human plasminogen. II. A kinetic study of activation with trypsin, urokinase and streptokinase.. J. biol. Chem 1958; 233: 86 8 Dreyer W.J, Neurath H. The activation of chymotrypsinogen. Isolation and identification of a peptide liberated during activation.. J. biol. Chem 1955; 217: 527 9 Bickford A.F, Taylor Jr. F.B, Sheena R. Inhibition of the fibrinogen-plasmin reaction by omega-aminocarboxylic acids and alkylamines.. Biochim. biophys. Acta (Amst.) 1964; 92: 328 10 Norman P.S. Studies of the plasmin system. II. Inhibition of plasmin by serum or plasma.. J. exp. Med 1958; 108: 53 11 Schwick H.G. Biochemie der Fibrinolyse.. Thrombos. Diathes. haemorrh. (Stuttgart) 1967; 17: 22 Suppl. 12 Nanninga L.B, Guest M.M. On the interaction of fibrinolysin (plasmin) with the inhibitors, antifibrinolysin and soybean trypsin inhibitor.. Arch. Biochem 1964; 108: 542 13 Christensen L.R, MacLeod G.M. A proteolytic enzyme of serum: characterization, activation and reaction with inhibitors.. J. Gen. Physiol 1945; 28: 559 14 Alkjaersig N. Fibrinogen Degradation by Plasmin.. Fed. Proc 1966; 25: 446 15 Fletcher A.P, Alkjaersig N, Sherry S. The proteolysis of fibrinogen by plasmin: The identification of thrombin clottable fibrinogen derivatives which polymerize abnormally.. J. Lab. clin. Med 1966; 68: 780 16 Nanninga L.B, Guest M.M. Preparation and properties of anticoagulant split product of fibrinogen and its determination in plasma.. Thrombos. Diathes. haemorrh. (Stuttgart) 1967; 17: 440
