| Literature DB >> 1259923 |
A G Beattie, D Ogston, B Bennett, A S Douglas.
Abstract
Plasma contained two inhibitors of plasminogen activation by urokinase when fractioned by gel filtration on Sephadex G-200. The inhibitor in the lower molecular weight fractions was separate from the principal protease inhibitors of plasma: alpha1-antitrypsin, alpha2-macroglobulin, C1 inactivator and antithrombin III, and from factor XIII. This activation inhibitor was present in both plasma and serum and its recovery was not reduced by preincubating the serum for 6 h at 37 degrees C. Its inhibitory activity was stable for several days at 4 degrees C, and was enhanced in the presence of an increased saline concentration. Preparations of the inhibitor, active in a clot lysis system, failed to inhibit the esterase activity of urokinase on N-alpha-acetyl-glycyl-L-lysine methyl ester.Entities:
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Year: 1976 PMID: 1259923 DOI: 10.1111/j.1365-2141.1976.tb01883.x
Source DB: PubMed Journal: Br J Haematol ISSN: 0007-1048 Impact factor: 6.998