<原著>気管支肺胞洗浄液中の線溶系蛋白分解酵素について

概要

論文の詳細を見る
It has been said that there are proteolytic enzymes or their inhibitors in respiratory tract fluid, with respect to the fibrinolytic enzymes of blood which have relation to hemoptysis. Their physiologic and pathophysiologic significance has not yet been known. In this study, a fibrinolytic enzyme in the soluble fraction of human bronchoalveolar lavage fluid (BALF) was analyzed. Sodium dodecyl sulfatepolyacrylamide get electrophoresis (SDS-PAGE) and enzymography of the fibrinolytic enzyme revealed that its molecular weight was 58,000. From the enzymic activity relation with diisoprophylfluophosphate (DFP), this enzyme was thought to belong to serine proteinase. Enzymic activity was inhibited by DTT, 2-mercaptoethanol, aprotinin, SBTI and UTI, but not inhibited by benzamidine, EDTA, TLCK, TPCK, EACA, pepstatin, kimostatin and antipain. But this enzyme was adsorbed on a fibrin Sepharose, showing no fibrin affinity. In amidolytic activity with S-2444 and S-2288,synthetic substrates, enhancement in absorbance due to the reaction with S-2288 was assumed to be the same reaction to TPA. When reacted with urokinase (UK) IgG antibody, it lost the enzymic activity, but showed no reaction with an antibody tissue plasminogen activator (TPA).
近畿大学の論文
1985-09-25