Separation of plasminogen activator by atfinity-chromatography on cetraxate-agarose

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It is known that the plasminogen activator of a certain type is an esterase for methylester of lysine or arginine. And we reported the method of isolating urokinase and other plasminogen activators, also by choosing lysine-agarose and arginine-agarose as the affinity-chromatography. Recently, we contrived a method which isolate urokinase, thrombin, plasmin, and plasminogen using affinity-chromatography on cetraxate-agarose. Cetraxate, one of methyl-ester of lysine and activator inhibitor, was produced by Fujii, Yamaura and others in 1971. So we would like to report them here.The results were as following.1; Urokinase was adsorbed to cetraxate-agarose, and was eluted with 0.005M phosphate buffer containing 0.85% NaCl.2; Cetraxate-agarose seemed to have a possibility of the separation of plasmin from the mixture of plasmin and plasminogen.3; It was suggested that affinity-chromatography on the inhibior-agarose has a possibility of discrimination between reversible and irreversible inhibition mechanism.
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