[Physicochemical and kinetic characteristics of myeloperoxidase of cow neutrophilic leucocytes].
Myeloperoxidase (MPO) isolated from granular fraction of cow peritoneal neutrophils had the RZ value equalled to 0.79. The absorption spectrum of MPO possesses characteristic bands at 430, 500, 570, 625, 690 nm. The molecular weight and sedimentation constant of the enzyme are 135.000-140.000 Daltons and 7.9S, respectively. The data obtained demonstrate the high thermostable property of MPO. Investigations of the pH optimum and effects of varying H2O2, o-dianizidine and MPO concentrations are described.
D000818:Animals; D002417:Cattle; D004355:Drug Stability; D005260:Female; D007700:Kinetics; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology*; D009195:Peroxidase / Q000097:blood*; D010544:Peroxidases / Q000097:blood*; D013053:Spectrophotometry
D010544:Peroxidases; D009195:Peroxidase
Fiziko-khimicheskie i kineticheskie kharakteristiki mieloperoksidazy neĭtrofil'nykh leĭkotsitov korov.