THERMODYNAMIC PARAMETERS FOR COMPLEX-FORMATION BETWEEN FIBRONECTIN OFBLOOD-PLASMA AND MYELOPEROXIDASE

Previous studies have demonstrated that fibronectin immobilized on BrC N-activated agarose binds soluble myeloperoxidase. The strength of the interaction is increased for fibronectin bound to immobilized gelatin e, its natural ligand. The thermodynamic characteristics of the intera ction of myeloperoxidase with fibronectin-gelatine-agarose are reporte d here. The proposed roles for the fibronectin-myeloperoxidase interac tion in inflammation loci include loading of phagocytes with the enzym e and protecting body tissues against extracellular myeloperoxidase-ge nerated oxidizing agents.