Title of article :
A linearization method for low catalytic activity enzyme kinetic analysis Original Research Article
Author/Authors :
Paolo Toti، نويسنده , , Antonella Petri، نويسنده , , Valerio Pelaia، نويسنده , , Ahmed M. Osman، نويسنده , , Moreno Paolini، نويسنده , , Carlo Bauer، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Abstract :
A kinetic analysis was made and a linear plot based on the general rate equation derived by Laidler [Can. J. Chem. 33, 1614–1624] is proposed. This linearization method allows determining the kinetic parameters (Km, kcat) and [E]0 for enzymes with low catalytic activity. The method was applied to chloroperoxidase from Caldariomyces fumago [EC 1.11.1.10], whose kinetic parameters Kmapp, kcatapp, and [E]0 with monochlorodimedone as substrate, were obtained by using the linearization plot and the Vmax value (calculated by Eadie–Hofstee plot).
This plot could also be useful to the study of abenzyme kinetics provided the concentration of the latter is either higher or equal than Km value.
Keywords :
Kinetic parameters , Chloroperoxidase , Catalytic antibody , Michaelis–Menten equation , Linear plot
Journal title :
Biophysical Chemistry
Journal title :
Biophysical Chemistry