The Mechanism of Activation of Cat Plasma by Streptokinase*

G Mootse; L.B Fleming; E.E Cliffton

doi:10.1055/s-0038-1654890

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1965; 14(03/04): 562-579
DOI: 10.1055/s-0038-1654890

Originalarbeiten — Original Articles — Travaux Originaux

Schattauer GmbH

The Mechanism of Activation of Cat Plasma by Streptokinase*

Autor*innen

G Mootse¹

¹Division of Experimental Surgery and Physiology, Sloan-Kettering Institute for Cancer Research; Cornell University Medical College, New York, N. Y. and the University of Newcastle Upon Tyne, England
L.B Fleming²

¹Division of Experimental Surgery and Physiology, Sloan-Kettering Institute for Cancer Research; Cornell University Medical College, New York, N. Y. and the University of Newcastle Upon Tyne, England
E.E Cliffton³

¹Division of Experimental Surgery and Physiology, Sloan-Kettering Institute for Cancer Research; Cornell University Medical College, New York, N. Y. and the University of Newcastle Upon Tyne, England

Abstract

Summary

1. The mechanism involved in the inactivation of cat plasma, serum, and plasma euglobulin by different concentrations of SK has been demonstrated.

2. Two different caseinolytic entities were graphically differentiated. They were characterized by their time of formation and stability studies.

3. With suboptimal SK concentration the development of the caseinolytic activity consisted of an initial rapid phase, followed by a slowly rising activity ; beta plasmin. With optimal SK concentration only the initial rapid caseinolytic activity was obtained (alpha plasmin).

4. It is suggested that beta plasmin was formed by a reversible reaction and was inactivated when substrate was not present. With increasing SK concentration alpha plasmin formation competed with the beta plasmin formation.

5. A comparison of potential caseinolytic activity of cat plasma, serum, and plasma euglobulin to beta and alpha plasmin is present.

Volltext

Referenzen

References
1 Mullertz S. Formation and properties of the activator of plasminogen and of human and bovine plasmin. Biochem. J. 61: 424 1955;
2 Astrup T. Fibrinolysis in the organism. Blood. 11: 781 1956;
3 Ablondi F. B, Hagen J. J. Comparison of certain properties of human plasminogen and “proactivator”. Proc. Soc. exp. Biol. (N. Y) 95: 195 1957;
4 Kline D. L, Fishman J. B. Proactivator function of human plasmin as shown by lysine esterase assay. J. Biol. Chem. 236: 2807 1961;
5 Zylber J, Blatt W. F, Jensen H. Mechanism of bovine plasminogen activation by human plasmin and streptokinase. Proc. Soc. exp. Biol. (N.Y) 102: 755 1959;
6 Markus G, Ambrus G. M. On the formation of different types of plasmin by streptokinase activation. J. biol. Chem. 235: 1673 1960;
7 Guest M. M, Geländer D. R. Assay of human plasma prokinase. Amer. J. Physiol. 187: 602 1956;
8 Ablondi F. B, Hagan J. J. Studies on specificity of streptokinase. Proc. Soc. exp. Biol. (N.Y) 99: 769 1961;
9 Alkjaersig N, Fletcher A. P, Sherry S. The mechanism of clot dissolution by plasmin. J. clin. Invest. 38: 1086 1959;
10 Troll W, Sherry S. Activation of human plasminogen by SKI. J. biol. Chem. 213: 881 1955;
11 Alkjaersig N, Fletcher A, Sherry S. A kinetic study of activation with trypsin, urokinase and SK. J. biol. Chem. 233: 86 1958;
12 Lassen M. The reaction between SK and human plasma. Acta chem. scand. 13: 1332 1959;
13 Norman P. S, Hill B. M. Studies of the plasmin system. III. Physical properties of the two plasmin inhibitors in plasma. J. exp. Med. 108: 639 1958;