Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma

FEBS Letters

Almquist, Åsa¹  Sigurdardottir, Olöf¹  Wiman, Björn¹  Lindahl, Tomas¹ 

[1] Department of Clinical Chemistry, Karolinska Hospital, S-104 01 Stockholm, Sweden

关键词: Plasminogen activator inhibitor;    Vitronectin;    Protein-protein interaction;    Fibrinolysis;   

DOI  :  10.1016/0014-5793(88)80999-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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. NH₂-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.

【 授权许可】

Unknown