Functionally active plasminogen activator inhibitor 1 (PAl) is bound to a discrete binding protein in plasma [(1988) Thromb. Haemost. 59, 392-395]. The binding protein has now been partially purified using conventional chromatographic techniques. After addition of active PAl its complex with the binding protein was purified by chromatography on insolubilized monoclonal antibodies towards PAl. Dodecylsulphate (polyacrylamide gel electrophoresis revealed two main compounds with molecular masses of 50 and 75 kDa respectively. Nl-I2-terminal amino acid sequence analysis and immunoblotting analysis suggested that the two compounds were PAl (50 kDa) and vitronectin (75 kDa). We conclude that the PAl-binding protein is identical to vitronectin.Plasminogen activator inhibitor; Vitronectin; Protein-protein interaction; Fibrinolysis

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