RSS-Feed abonnieren
DOI: 10.1055/s-0038-1647852
Streptokinase Stability Pattern during Storage in Various Solvents and at Different Temperatures[*]
Publikationsverlauf
Received 29. Oktober 1974
Accepted 02. März 1975
Publikationsdatum:
24. Juli 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/197501/lookinside/thumbnails/10-1055-s-0038-1647852-1.jpg)
Summary
The activity drop of 5 u streptokinase was measured in 1 ml each of various solutions (0.9% NaCl solution, 5% glucose solution, 5% levulose solution, 10% dextran solution, gelatin solution, 3% albumin solution, Michaelis buffer, glucose (5%)-heparin (750 u/ml) solution) at different incubation temperatures (–20° c, 4° c, 20 c, 37 C), and over different observation periods (15 min, 30 min, 45 min, 60 min, 6 h, 12 h, 24 h, and 48 h). Solution media tested for streptokinase-protecting quality were broken down into three groups.
Group I: Solvents displaying excellent stabilizing properties (gelatin and albumin solutions).
Group II: Solvents displaying medium stabilizing properties (dextran and levulose solutions).
Group III: Solvents displaying poor stabilizing properties (NaCl and glucose solutions, Michaelis buffer).
In testing streptokinase concentrations as used for therapeutic purposes (1500 u/ml, 50,000 u/ml), no decay was found to take place over observation periods of up to 48 h, and no influence by different solvents (Group I, II or III) was traceable. Heparin stored with streptokinase at room temperature over a period of 48 h did not alter the streptokinase stability.
Some mechanisms concerning the stability pattern of streptokinase are discussed. It appears that low streptokinase concentrations need negatively charged colloids to keep the protein structure intact. The streptokinase-protecting macro-molecules tested so far were albumin, gelatin, and streptokinase. Obviously, streptokinase by itself was able to preserve its own stability provided its concentration was of a certain order of magnitude (1500 u/ml, 50,000 u/ml).
* Supported by Grants from Verein zur Bekämpfung der Gefäßerkrankungen e. v., Engelskirchen.
-
References
- 1 Appel W. Chemie und Biochemie Klinischer Dextrane – 100 Jahre Dextran. Transactions of “Dextran Symposium” Krems|Austria . Ed Knoll AG. Chemische Fabriken: Ludwigshafen;
- 2 Auel H, Martin M. Plasminogengehalt eines im Handel befindlichen Rinderplasminogens. Zeitschrift für klinische Chemie 1974; 12: 385
- 3 Christensen L. R. Protamin purification of streptokinase and effect of pH and temperature on reversible inactivation. Journal of General Physiology 1947; 30: 465
- 4 Fischer A, Schmitz A. Über die Chemische Natur des Heparins. I. Die quantitative Bestimmung des Heparins. Zeitschrift für physiologische Chemie 1932; 210: 129
- 5 Hartert H. Die Thromboelastographie. Eine Methode zur physikalischen Analyse des Blutgerinnungsvorgangs. Zeitschrift für die gesamte experimentelle Medizin 1951; 117: 189
- 6 Von Kaulla K. N, McDonald T. S. The effect of heparin on components of the human fibrinolytic system. Blood 1958; 13: 811
- 7 Martin M. Studies on activator formation in human plasma with streptokinase. I. Experimental studies. Thrombosis et Diathesis Haemorrhagica 1973; 30: 381
- 8 Martin M. Indirect measurement of streptokinase concentration in the plasma of patients undergoing fibrinolytic treatment. Thrombosis et Diathesis Haemorrhagica 1974; 32: 633
- 9 Martin M, Schoop W, Zeitler E. Streptokinase in chronic arterial occlusive disease. Journal of the American Medical Association 1970; 211: 1169
- 10 Zekorn D. Chemische und biochemische Eigenschaften der Plasmaersatzpräperate auf Gelatinbasis. In Horatz K. (ed.) Plasmaersatzpräparate auf Gelatinbasis . Stuttgart: Georg Thieme Verlag; 1 1968