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  • Title: [Isolation and characteristics of urokinase-type plasminogen activator from a culture of human embryo lung fibroblasts].
    Author: Shevelev AIa, Barshevskaia TN, Belogurov AA, Kratasiuk GA, Goriunova LE.
    Journal: Mol Biol (Mosk); 1986; 20(3):778-88. PubMed ID: 3088432.
    Abstract:
    Plasminogen activator from conditioned medium of human embryonal lung fibroblasts was purified by phosphocellulose P11 chromatography, followed by p-aminobenzamidine-agarose chromatography. Two forms of plasminogen activators were separated by chromatography on the heparin-sepharose. The high molecular weight form (53 kDa) with specific activity 130 000 IU/mg consists of two polypeptide chains (31 kDa and 20 kDa) and exhibits strong affinity for fibrin-celite, lysine-sepharose and heparin-sepharose. The low molecular weight form (32 kDa, 190 000 IU/mg) also binds to these sorbents, but more weakly, and its properties are very similar to those of low molecular weight urokinase. Activity of both forms of plasminogen activators are inhibited by monoclonal antibodies against urokinase. A number of enzymological chromatographic and immunological properties indicates, that the plasminogen activator from lung fibroblasts is of urokinase type.
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