Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme.

Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin. The electrophoretic mobility of mixtures of MPO and heparin in polyacrylamide gels under nondenaturing conditions was consistent with a strong interaction of the cationic enzyme with the polyanionic polysaccharide. Purified MPO prebound to bovine aorta endothelial cells (BAEC) and supplemented with hydrogen peroxide dose- and time-dependently abrogated the interaction of coagulation factor IX (FIX) with factor IX-binding protein (FIXBP) on the surface of BAEC reflecting oxidative modification of the binding protein.