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1.
Vopr Med Khim ; 42(2): 137-40, 1996.
Artigo em Russo | MEDLINE | ID: mdl-9148599

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/sangue
2.
Biokhimiia ; 60(8): 1217-20, 1995 Aug.
Artigo em Russo | MEDLINE | ID: mdl-7578576

RESUMO

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.


Assuntos
Fibronectinas/sangue , Peroxidase/sangue , Cromatografia de Afinidade , Gelatina/química , Fagócitos/enzimologia , Sefarose/química , Temperatura , Termodinâmica
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