[Thermodynamic parameters of complex formation of blood plasma fibronectin and myeloperoxidase].
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.
Iankovskiĭ
O Iu
OIu
Khilazhetdinova
L R
LR
Kokriakov
V N
VN
Aleshina
G M
GM
Iablunovskaia
I A
IA
Podsukhina
G M
GM
Gavrilova
Iu V
IuV
Leonova
N V
NV
D002846:Chromatography, Affinity; D005353:Fibronectins / Q000097:blood*; D005780:Gelatin / Q000737:chemistry; D009195:Peroxidase / Q000097:blood*; D010586:Phagocytes / Q000201:enzymology; D012685:Sepharose / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics
D005353:Fibronectins; D005780:Gelatin; D012685:Sepharose; D009195:Peroxidase
Termodinmicheskie parametry kompleksoobrazovaniia fibronektina plazmy krovi i mieloperoksidazy.