Fibrinolytic Activation of Plasma by Means of Urokinase in Vitro and in Vivo

L. B Nanninga; M. M Guest

doi:10.1055/s-0038-1654208

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1970; 24(01/02): 033-042
DOI: 10.1055/s-0038-1654208

Originalarbeiten – Original Articles – Travaux Originaux

Schattauer GmbH

Fibrinolytic Activation of Plasma by Means of Urokinase in Vitro and in Vivo

L. B Nanninga

¹Department of Physiology, University of Texas Medical Branch, Galveston, Texas

,

M. M Guest^*

¹Department of Physiology, University of Texas Medical Branch, Galveston, Texas

› Author Affiliations

Abstract

Summary

The activation of plasma by urokinase was studied in vitro by measuring the levels of fibrinogen, the anticoagulant split product of fibrinogen and the level of profibrinolysin. It is concluded that normal plasma contains about one CTA unit of plasmakinase, expressed in urokinase equivalents. The level of free fibrinolysin after complete activation of profibrinolysin was estimated to be approximately one-tenth of the initial profibrinolysin concentration. The split product of fibrinogen is present as an intermediate in a consecutive reaction in amounts dependent on the concentration of the activator present.

Full Text

References

References
1 Nanninga L. B, Guest M. M. Antifibrinolytic action of the anticoagulant split product of fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg) 19: 526 1968;
2 Maxwell R. E, Nickel V. S, Lewandowski V. Preparations of plasminogen deficient fibrinogen and thrombin. Biochem. biophys. Res. Commun 07: 50 1962;
3 Nanninga L. B, Guest M. M. Activity-pH relationship and Michaelis constants during activation of profibrinolysin and during fibrinogenolysis. Thrombos. Diathes. haemorrh. (Stuttg) 19: 492 1968;
4 Ware A. J, Guest M. M, Seegers W. H. Fibrinogen; with special reference to its preparation and certain properties of the product. Arch. Biochem 13: 231 1947;
5 Nanninga L. B, Guest M. M. Preparation and properties of the anticoagulant split product of fibrinogen and its determination in plasma. Thrombos. Diathes. haemorrh. (Stuttg) 17: 440 1967;
6 Nanninga L. B. Rapid determination of profibrinolysin (plasminogen) in plasma. Thrombos. Diathes. haemorrh. (Stuttg) 17: 8 1967;
7 Robbins K. C, Summaria L, Hsieh B, Shah R. J. The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin. J. biol. Chemistry 242: 2333 1967;
8 Nanninga L. B, Guest M. M. Rapid determination of antifibrinolysin (antiplasmin) in plasma. Thrombos. Diathes. haemorrh 15: 273 1966;
9 Schwick H. G. Biochemie der Fibrinolyse. Thrombos. Diathes. haemorrh. (Stuttg) 17, Suppl 22: 28 1967;
10 Norman SPh. Studies on the plasmin system. I. Measurement of human and animal plasminogen. Measurement of an activator in human serum. J. exp. Med 106: 423 1957;
11 Fletcher A. P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (fibrinolytic) states. I. The significance of fibrinogen proteolysis and circulating fibrinogen breakdown products. J. clin. Invest 41: 896 1962;
12 Amris A, Amris C. J. Turnover and distribution of ¹³¹iodine labelled human fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg) 11: 404 1964;
13 Hart C. hH, Meeuwissen T. hOJA. La demi-vie biologique du fibrinogène marqué a l’aide d’iode radioactif (I¹³¹) dans les cas d’hypercholesterolémie et d’affections vasculaires arterielles. Coagulation 01: 71 1968;
14 Ferguson E. W. Effects of exercise and physical conditioning on hemostatic mechanisms. Thesis, University of Texas Medical Branch; Galveston, Texas, 1969.:
15 Schwick H. G. Immunochemistry of fibrinogen. Thrombos. Diathes. haemorrh. (Stuttg.) Suppl 13: 85 1964;
16 Das P. G, Allan A. G. E, WoocLfield D. G, Gash J. D. Fibrin degradation products in sera of normal subjects. Brit. med. J 1967; part 4, 718.
17 Latallo Z. S, Fletcher A. P, Alkjaersig N, Sherry S. Inhibition of fibrin polymerization by fibrinogen proteolysis products. Amer. J. Physiol 202: 681 1962;
18 Bang N. U, Fletcher A. P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (fibrinolytic) states. III. Demonstration of abnormal clot structure by electron microscopy. J. clin. Invest 41: 935 1962;
19 Nolf P. Des modifications de la coagulation du sang chez le chien après extirpation du foie. Arch. int. Physiol 03: 1 1905;
20 Astrup T. In: Connective Tissue, Thrombosis and Atherosclerosis. Page I. H. editor. Academic Press; 1959: 224.
21 Copley A. L. In: Flow Properties of Blood. Ed. Copley A. L, Stainsby G. Pergamon Press; 1960
22 Gitlin D, Borges W. H. Studies on the metabolism of fibrinogen in two patients’with congenital afibrinogenemia. Blood 08: 679 1953;
23 Nanninga L. B, Guest M. M, Dickie K. J, de Groot W. J, Bond T. The appearance of fibrinogen derivatives in thromboembolic disease after treatment with urokinase. XII Congress International Soc. of Hematology. New York: 1968
24 Niléhn J. E. Split products of fibrinogen after prolonged interaction with plasmin. Thrombos. Diathes. haemorrh. (Stuttg) 18: 89 1967;