[Thermodynamic parameters of complex formation of blood plasma fibronectin and myeloperoxidase]

Abstract

Previous studies have demonstrated that fibronectin immobilized on BrCN-activated agarose forms a complex with soluble myeloperoxidase. The affinity of such interaction increases after preliminary absorption of fibronectin on a column with immobilized gelatin, one of its natural ligands. The thermodynamic characteristics of the myeloperoxidase interaction with fibronectin-gelatin-agarose have been established. The role of fibronectin-myeloperoxidase interaction in the inflammation focus is discussed in terms of the mode of the phagocyte loading with the enzyme and as a way of protecting intrinsic body tissues from injury by oxidants generated by extracellular myeloperoxidase.