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

FEBS Lett. 1988 Dec 19;242(1):125-8. doi: 10.1016/0014-5793(88)80999-2.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Blood Proteins
  • Chromatography
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / blood*
  • Glycoproteins / isolation & purification
  • Humans
  • Immunoblotting
  • Molecular Sequence Data
  • Molecular Weight
  • Plasminogen Activators / antagonists & inhibitors
  • Plasminogen Inactivators
  • Vitronectin

Substances

  • Blood Proteins
  • Glycoproteins
  • Plasminogen Inactivators
  • Vitronectin
  • Plasminogen Activators