N-oleoyl heparin inhibits the amidolytic activity of plasmin and urokinase.
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.
Legras
S
S
Laboratoire de Biologie du Tissu Conjonctif, CNRS URA 1460, Créteil, France.
Diczhazi
C
C
Moczar
M
M
D000577:Amides / Q000378:metabolism; D000818:Animals; D005341:Fibrinolysin / Q000037:antagonists & inhibitors*; D006493:Heparin / Q000031:analogs & derivatives* / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D009829:Oleic Acids / Q000494:pharmacology*; D013552:Swine; D014568:Urokinase-Type Plasminogen Activator / Q000037:antagonists & inhibitors*
D000577:Amides; D009829:Oleic Acids; C072705:oleoyl heparin; D006493:Heparin; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator