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Thrombolytic Properties of Staphylokinase

We evaluated the properties of recombinant staphyloki-nase in comparison with those of tissue-type plasminogen activator (t-PA) and streptokinase (SK). The presence of fibrin(ogen) fragment FCB-2 in the reaction mixture increased plasminogen activation by staphylokinase more than 20-fold. Such chara...

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Bibliographic Details
Published in:Blood 1990-09, Vol.76 (5), p.925-929
Main Authors: Matsuo, Osamu, Okada, Kiyotaka, Fukao, Hideharu, Tomioka, Yoshiki, Ueshima, Shigeru, Watanuki, Masaaki, Sakai, Masashi
Format: Article
Language:English
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Summary:We evaluated the properties of recombinant staphyloki-nase in comparison with those of tissue-type plasminogen activator (t-PA) and streptokinase (SK). The presence of fibrin(ogen) fragment FCB-2 in the reaction mixture increased plasminogen activation by staphylokinase more than 20-fold. Such characteristics are similar to those of t-PA. On the other hand, SK was not affected by the presence of FCB-2. The thrombolytic properties of staphy-lokinase were studied in a system consisting of a radioactive human plasma clot (125l-fibrinogen-labeled) suspended in the circulating citrated plasma. Significant thrombolysis (50% in 3 hours) was obtained with 2 μg/mL of staphyloki-nase and 4.45 μg/mL t-PA, as compared with 12  μ g/ml. for SK. The relative molar potency of staphylokinase, calculated from the molecular weight, was about two times more effective than that of SK, but about half of that of t-PA. Systemic fibrinolytic activation and fibrinogen break-down was not observed with staphylokinase or t-PA, but was observed with SK. The thrombolytic efficiency of staphylokinase, which was calculated as the ratio of the degree of thrombolysis/the degree of fibrinogenolysis, was about five times greater than that of SK, and about half of that of t-PA. These findings suggest that staphylokinase has higher specific thrombolytic properties and lesser fibrinogenolytic properties than those of SK.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V76.5.925.925