N-oleoyl heparin inhibits the amidolytic activity of plasmin and urokinase

Int J Biol Macromol. 1992 Apr;14(2):97-9. doi: 10.1016/0141-8130(92)90005-s.

Abstract

N-desulphated heparin, partially N-acylated on average with three oleoyl chains per molecule, inhibits the amidolytic activity of plasmin (IC50 16 nM) and urokinase (IC50 10mM) when assayed on N-p-tosyl-Gly-Pro-Lys-4-nitroanilide and benzoyl-Ala-Gly-Arg-4-nitroanilide substrates respectively. N-desulphated heparin is not inhibitory. This effect requires the covalent binding of oleoyl residues to heparin and it decreases with increasing concentration of Tris-HCl and non-ionic detergents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / metabolism
  • Animals
  • Fibrinolysin / antagonists & inhibitors*
  • Heparin / analogs & derivatives*
  • Heparin / pharmacology
  • Humans
  • Kinetics
  • Oleic Acids / pharmacology*
  • Swine
  • Urokinase-Type Plasminogen Activator / antagonists & inhibitors*

Substances

  • Amides
  • Oleic Acids
  • oleoyl heparin
  • Heparin
  • Fibrinolysin
  • Urokinase-Type Plasminogen Activator