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Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma
Author(s) -
Wiman Björn,
Almquist Åsa,
Sigurdardottir Olöf,
Lindahl Tomas
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80999-2
Subject(s) - vitronectin , plasminogen activator inhibitor 1 , chemistry , plasminogen activator , microbiology and biotechnology , biochemistry , medicine , biology , integrin , receptor
Functionally active plasminogen activator inhibitor 1 (PAI) 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 PAI its complex with the binding protein was purified by chromatography on insolubilized monoclonal antibodies towards PAI. Dodecylsulphate (polyacrylamide gel electrophoresis revealed two main compounds with molecular masses of 50 and 75 kDa respectively. NH 2 ‐terminal amino acid sequence analysis and immunoblotting analysis suggested that the two compounds were PAI (50 kDa) and vitronectin (75 kDa). We conclude that the PAI‐binding protein is identical to vitronectin.