[Kinetic properties and heat resistance of the peritoneal leukocyte myeloperoxidase of white mice].
The dependence of the myeloperoxidase-catalyzed reaction in the concentration of the enzyme and that of both substrates (hydrogenperoxide and o-dianizidine) was investigated. The substrates--velocity curves appeared non-hyperbolic, an inhibitory effect was registered for both substrates. Hill coefficient with a varying value was employed to characterize the deviation of the curves from Michaelis--Menten hyperbolas apparently caused by the interaction of non-identical subunits composing the enzyme molecule. The effect of the preincubation temperature on the enzyme activity and the kinetics of thermoinactivation of the enzyme are analysed, the purified enzyme preparation being more thermostable than the crude one.
D000818:Animals; D001202:Ascitic Fluid / Q000166:cytology*; D002384:Catalysis; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D051379:Mice; D009195:Peroxidase; D010544:Peroxidases; D013696:Temperature
D010544:Peroxidases; D009195:Peroxidase
Issledovanie kineticheskikh svoĭstv i teploustoĭchivosti mieloperoksidazy peritoneal'nykh leĭkotsitov belykh mysheĭ