[Change in the kinetic properties of NAD-kinase from pigeon heart muscle during purification].
Partially purified preparations of pigeon heart NAD-kinase reveal a complex kinetic behaviour in a catalyzed reaction; the curve for the dependence of the initial reaction rate on substrate concentration has a intermediate plateau and a maximum. The shape of the kinetic curve and the specific activity of the enzyme preparations depend on protein concentration as well as on the time and conditions of enzyme storage. The electrophoretically homogeneous preparations of NAD-kinase demonstrate a hyperbolic dependence of the NADP synthesis rate on substrate concentration and a loss of dependence of specific activity on the enzyme concentration. The interrelationship between the changes in the kinetic parameters of NAD-kinase and the quaternary structure of the enzyme during purification is discussed.
D000818:Animals; D010856:Columbidae; D007700:Kinetics; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology*; D009249:NADP / Q000032:analysis; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor)
D046911:Macromolecular Substances; D009249:NADP; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C021844:NAD kinase
Izmenenie kineticheskikh svoĭstv NAD-kinazy iz serdechnoĭ myshtsy golubia v protsesse ochistki.