Blood & Vessel
Online ISSN : 1884-2372
Print ISSN : 0386-9717
Separation of plasminogen activator by atfinity-chromatography on cetraxate-agarose
Tadaaki SHIBASetsuo TAKEUCHITakeru TERASHIMAKazuhiro KUBOTAJun TAKATSUKAYuzo URITAHiroki OZAWAKyoei NONAKASaburo AWAZUMichiko IGARASHIToshio ASADA
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1978 Volume 9 Issue 2 Pages 281-285

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Abstract

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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© The Japanese Society on Thrombosis and Hemostasis
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