Thromb Haemost 1977; 38(01): 307
DOI: 10.1055/s-0039-1682434
Supplemental Abstracts
Schattauer GmbH

Isolation and Properties of Human Vascular Plasminogen Activator

R. Allen
1   S.E. Scotland Regional Blood Transfusion Service, Edinburgh, Scotland
,
D.S. Pepper
1   S.E. Scotland Regional Blood Transfusion Service, Edinburgh, Scotland
,
J.D. Cash
1   S.E. Scotland Regional Blood Transfusion Service, Edinburgh, Scotland
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Publikationsdatum:
16. April 2019 (online)

 

    The vascular tree of cadaver legs was washed out with a detergent - glucose mixture and the soluble activator precipitated with 8%PEG 6,000. The redissolved precipitate was chromatogranhed on 4% agarose where it exhibited an apparent molecular weight of 8 × 105 and was well resolved from lipids, factor VIII antigen, albumin and haemoglobin. The active material eluted in the void volume of G-200 Sephadex when using 0.15 M NaCl eluant, but was dissociated and retarded by re-chromatography in 1 M NaCl or lysine. The dissociated, purified enzyme had an apparent molecular weight of 56,000 and was a serine protease. The enzymic activity of the carrier complex was stable for several days at 4°C, but the dissociated enzyme was rapidly inactivated at 4°C.


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