RESUMO
Human blood plasma fibronectin immobilised on agarose in physiological interacts with soluble myeloperoxidase (Kd = 2.43 mM). Interaction of myeloperoxidase with fibronectin adsorbed on immobilised gelatin a, natural fibronectin ligand, resulted in formation more stable complex (Kd = 0.94 mM). The presence of thermoaggregated (but not native) IgG in the liquid phase increased a stability of the complex (0.06 mM). It is suggested that myeloperoxidase could represent a component of complex super molecular structure, real immune complex.
Assuntos
Fibronectinas/química , Peroxidase/química , Fibronectinas/sangue , Humanos , Imunoglobulina G/química , Cinética , Ligantes , Substâncias Macromoleculares , Peroxidase/sangueRESUMO
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.