The interaction of human α2-Macroglobulin with fibrinolytic enzymes
| Autor: | Yoko Ito, Hiroyasu Yamamoto, Isamu Sugie, Kazuo Ichikawa |
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| Rok vydání: | 1978 |
| Předmět: | |
| Zdroj: | Blood & Vessel. 9:84-88 |
| ISSN: | 1884-2372 0386-9717 |
| DOI: | 10.2491/jjsth1970.9.84 |
| Popis: | The comparative action of purified human α2M on fibrinolytic enzymes, euglobulin, plasmin, urokinase and proactivator has been investigated. The aim of this investigation was to determine inhibition sites and rate on fibrinolytic enzymes system, further to study whether or not inhibitory action was different with several substrates, bovine standard plate (BSP), bovine plasminogen free fibrin plate (BfP), casein and AGLME.RESULTS1, α2M markedly extended euglobulin lysis time.2. α2M inhibited fibrinolytic activity of Eug+SK and Eug+UK on BSP and BfP. Of special interest was that inhibition percent of α2M to plasminogen activator and plasmin was different.3. Plasminogen activator and AGLME esterase activities of proactivator-SK complex were not affected by α2M.4. α2M inhibited plasminogen activator and AGLME esterase activities of urokinase.5. α2M inhibited fibrinolytic activity and caseinolytic activity of plasmin. The inhibition rate of the former was larger than the latter.6. It was calculated that 6.4-14.3 INU (BSP), 53.2 INU (AGLME) of UK and 0.82 CU (BfP), 0.6CU (Casein) of plasmin was inhibited by one mg of α2M.These results are summarized in Table 1. |
| Databáze: | OpenAIRE |
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