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Urokinase has been applied to hypercoagulative diseases as a plasminogen activatng enzyme. There has, however, been a divergence of opinion as to its clinical effectiveness because of its instability and susceptibility towards urokinase inhibitors present in plasma.Enzymatic stability in vitro and resistance to those inhibitors are provided to native urokinase by chemical modification with monomethoxypolyethylene glycol #5000 activated with cyanuric chloride. The modified urokinase showed elevated and elongated in vivo activity, namely prominent consumption of plasmin inhibitor and plasminogen in normal rabbits compared to native one.
- 一般社団法人 日本血栓止血学会の論文
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