Abstract:
:The relative fibrin-binding, fibrinolytic and fibrinogenolytic properties of single-chain pro-urokinase, an inactive proenzyme form of human urokinase purified from cultured human kidney cells, and urokinase were compared. The affinity of single-chain pro-urokinase for fibrin was much higher than that of urokinase. In Vitro thrombolytic studies showed that single-chain pro-urokinase is approximately three times more potent in fibrinolysis than urokinase and that it does not degrade fibrinogen in the plasma at a concentration, at which complete plasma clot lysis takes place; whereas, urokinase extensively degrades the fibrinogen in the plasma. These specific, potent thrombolytic properties of single-chain pro-urokinase seem to be due to its high affinity for fibrin and to its conversion from the inactive single-chain form to the active two-chain form on the thrombus by the catalytic amount of plasmin generated during coagulation. This single-chain pro-urokinase obtained from human kidney cells by tissue culture should prove advantageous than urokinase in thrombolytic therapy.
journal_name
Cell Struct Functjournal_title
Cell structure and functionauthors
Kasai S,Arimura H,Nishida M,Suyama Tdoi
10.1247/csf.10.151subject
Has Abstractpub_date
1985-06-01 00:00:00pages
151-9issue
2eissn
0386-7196issn
1347-3700journal_volume
10pub_type
杂志文章abstract::In this study, we measured hydrogen peroxide (H2O2) release as one of the functions of mature eosinophils, and utilized it as a quantitative index. We demonstrated that 1) the human eosinophilic leukemia cell line, EoL-1, did not release H2O2 when stimulated with phorbol myristate acetate (PMA), but after culturing wi...
journal_title:Cell structure and function
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pub_type: 杂志文章
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更新日期:2002-12-01 00:00:00
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pub_type: 杂志文章,评审
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