Thrombosis and Haemostasis, Table of Contents Thromb Haemost 1966; 15(01/02): 273-283DOI: 10.1055/s-0038-1649427 Originalarbeiten — Original Articles — Travaux Originaux Schattauer GmbH Rapid Determination of Antifibrinolysin (Antiplasmin) in Plasma[*] 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› Author AffiliationsRecommend Article Abstract Buy Article Summary A nephelometric assay of antifibrinolysin in plasma is described. This assay is based on the inhibition of fibrinogenolysis. An equation is derived to calculate the antifibrinolysin content. Only the activity of the rapid acting antifibrinolysin is obtained. The values for antifibrinolysin are given in mol/L based on a molecular weight 57.000 (1). All values are based (standardized) on the inhibition of fibrinolysin by crystalline soybean trypsin inhibitor. Full Text References References 1 Nanninga L. B, Guest M. M. On the interaction of fibrinolysin (plasmin) with the inhibitors antifibrinolysin and soybean trypsin inhibitor. Arch. Biochem. Biophys 108: 542 1964; 2 Ware A. G, Guest M. M, Seegers W. H. Fibrinogen: with special reference to its preparation and certain properties of the product. Arch. Biochem. Biophys 13: 231 1947; 3 Guest M. M, Daly B. M, Ware A. G, Seegers W. H. A Study of antifibrinolysin activity in the plasma of various animal species. J. clin. Invest 27: 785 1948; 4 Nanninga L. B, Guest M. M. Blocking of inhibition of fibrinolysin by mercurials and oxidizing agents. Arch. Biochem. Biophys 109: 607 1965; 5 Blix S. The stability of fibrinolytic inhibitors in human serum and the inhibitor content in animal sera. Scand. J. clin. Lab. Invest 16: 614 1964; 6 de Wit Dudok C. Investigation on the inhibitors of the fibrinolytic system. Thrombos. Diathes. haemorrh. (Stuttg) 12: 105 1964; 7 Nanninga L. B. Fibrinogen: preparation, photoelectric determination, molecular weight, viscosity, formol titration before and after clotting. Arch, néerl. Physiol 28: 241 1946; 8 Parfentjew I. A, Johnson M. L, Clijfton E. E. The determination of plasma fibrinogen by turbidity with ammonium sulphate. Arch. Biochem. Biophys 46: 470 1953; 9 Mihalyi E, Godfrey J. E. Digestion of fibrinogen by trypsin. Biochim. biophys. Acta (Amst) 67: 73-90 1963; 10 Seegers W. H, Nieft M, Vandenbelt J. M. Decomposition products of fibrinogen and fibrin. Arch. Biochem 07: 15 1945; 11 Niewiarowski S, Kowalski E. Un nouvel anticoagulant dérivé du fibrinogène. Rev. Hémat 13: 320 1958; 12 Triantaphyllopoulos E, Triantaphyllopoulos D. C. Variability of the anticoagulant fraction of incubated fibrinogen. Amer. J. Physiol 208: 521 1965; 13 Maki M. Anticoagulant activity of digest products of fibrinogen by plasmin Tohoku. J. exp. Med 84: 201 1964; 14 Ratnoff O. D. Fibrinogen and fibrin as substrates for the proteolytic enzyme of plasma. J. clin. Invest 32: 473 1953; 15 Christensen L. R. Streptococcal fibrinolysis: a proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin. J. gen. Physiol 28: 363 1944/45 16 Gajewski J, Alexander B. Effect of plasmin on fibrinogen and fibrin. Amer. J. Physiol 206: 79 1964; 17 Martin G. J. Inhibition of trypsin, chymotrypsin and plasmin by an inhibitor isolated from sheep serum. J. biol. Chem 237: 2099 1962; 18 Derechin M. The assay of human plasminogen with casein as substrate. Biochem. J 78: 443 1961; 19 Kunitz M. Crystalline soybean trypsin inhibitor. J. gen. Physiol 30: 291-311 1947; 20 Ronwin E. The active center of plasmin. Biochim. biophys. Acta (Arnst) 38: 258 1960; 21 Jansen E. F, Balls A. K. The inhibition of α and β chymotrypsin and trypsin by diisopro- pylfluorophosphate. J. biol. Chem 194: 721 1952; 22 Wu Y. V, Scheraga H. A. Studies of soybean trypsin inhibitor. I Physicochemical properties. Biochemistry 01: 698 1962; 23 Steiner R. F. The combination of trypsin with soybean inhibitor. Arch. Biochem. Biophys 49: 71 1954; 24 McLaren A. D. Some observations on a trypsin - trypsin inhibitor system. C.R. Lab. Carlsberg 28: 175 1952; 25 Alkjaersig N. A, Fletcher P, Sherry S. The mechanism of clot dissolution by plasmin. J. clin. Invest 38: 1086 1959; 26 Norman P. S. Studies of the plasmin system. II Inhibition of plasmin by serum or plasma. J. exp. Med 108: 53 1958; 27 Ablondi F. B, Hagan J. J, Philips M, De Renzo E. G. Inhibition of plasmin, trypsin and the streptokinase activated fibrinolytic system by ε aminocaproic acid. Arch. Biochem. Biophys 82: 153 1959; 28 McNicol G. P, Fletcher A. P, Alkjaersig N, Sherry S. The absorption distribution and excretion of e aminocaproic acid following oral and intravenous administration to man. J. Lab. clin. Med 59: 15 1962; 29 Sherry S, Fletcher A. P, Alkjaersig N, Sawyer W. D. ε aminocaproic acid: “a potent antifibrinolytic agent”. Trans. Ass. Amer. Phycns 72: 62 1959; 30 Alkjaersig N, Fletcher A. P, Sherry S. α aminocaproic acid: an inhibitor of plasminogen activation. J. biol Chem 234: 832 1959; 31 Bickford A. F, Taylor F. B, Sheena R. Inhibition of fibrinogen-plasmin reaction by co aminocarboxylic acids and alkylamines. Biochim. biophys. Acta (Amst) 92: 328 1964; 32 Robbins K. C, Summaria L, Elwyn D, Barlow G. H. Further studies on the purification and characterization of human plasminogen and plasmin. J. biol. Chem 240: 541 1965; 33 Nussenzweig V, Seligmann M. Analyse par des methodes immunochimiques de la degradation par la plasmine du fibrinogène humain et de la fibrine a different stades. Rev. Hémat 15: 451 1960;
