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.