<原著>組織性プラスミノーゲンアクチベータ(t-PA)の生化学的性質

概要

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We investigated the biochemical characteristics of tissue-type plasminogen activator (t-PA) in comparison with another urinary plasminogen activator, urokinase (UK). SDS-PAGE and enzymographical analysis of t-PA showed different molecular weights from those in UK. In addition, the isoelectric points of t-PA were pH 8.75-8.55,8.05,7.80 and 7.25 ; on the other hand, those of UK were pH 8.90,8.70,8.30 and 8.10. Amidolytic activities of t-PA were stronger in the chromogenic substrate S-2288 than those of S-2444,but the activities of UK were stronger in S-2444 than those in S-2288. Fibrin affinity was investigate by using fibrin-Sepharose column as well as adsorption to fibrin clot. UK passed through the fibrin-Sepharose column, but t-PA was adsorbed by the column which was eluted by 0.2M arginine solution. When radiolabeled UK was used to determine the affinity to fibrin clot, only 4% of both high molecular (55 K) and low molecular weight (33 K) UK was adsorbed. On the other hand, 35.7% of t-PA was adsorbed, demonstrating about 10-fold higher fibrin affinity than UK. Next, the affinity to lysine was investigated by performing lysine-Sepharose column chromatography. Although UK passed through the column, t-PA was adsorbed as in fibrin-Sepharose. These results indicate that t-PA has both fibrin binding site and lysine binding site, yet that UK has none of them.
近畿大学の論文
1986-03-25