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Vascular plasminogen activator (PA) is unstable and previous attempts at isolating it from blood have been hindered by the difficulty in separation it from inhibitors and other proteins. We studied its charactor by using a Fibrin/Celite column chromatography proposed by Husain et al. PA was partially purified by taking advantage of its strong binding to fibrin. The fraction eluted by 0.2M arginine showed plasminogen activator activity on fibrin plates. Determination of amidolytic activities on chromogenic substrate S-2251 (Kabi) in the presence of plasminogen and also on S-2288 were made. PA fraction showed high activities on them which were not influenced by Trasyrol, Soybean trypsin inhibitor, AT-III and Heparin. Plasminogen and plasmin inhibitors were not detected in the PA fraction but a small amount of factor XII, prekallikrein and high molecular weight kininogen were contaminated. By the method of SDS-PAGE, three bands, molecular weight 140, 000, 80, 000 and 66, 000 have been shown in the fraction and the main activity of PA was brought about by the protein corresponding to the band of molecular weight of 80, 000. Nevertheless the breakthrough also showed a high fibrinolytic activity which contained plasmin inhibitors. It seems that a different type of PA is present in the breakthrough.
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