Ill-conditioning associated with the "end-point" method for the determination of kinetic parameters describing irreversible enzyme inactivation by an unstable inhibitor.
Study of the complete time-course of irreversible enzyme inhibition by an unstable inhibitor yields more information than can be obtained by recording data only at the end point of reaction. Time-course analysis of co-operative irreversible enzyme inhibition by an unstable inhibitor has been shown to be considerably less susceptible to ill-conditioning than the "end-point" method for the determination of kinetic parameters describing inactivation. As a result, mechanisms that cannot be distinguished by the "end-point" method are readily differentiated by time-course analysis without the need to isolate intermediate species.
Topham
C M
CM
Department of Biochemistry, Medical College of St Bartholomew's Hospital, University of London, U.K.
D004791:Enzyme Inhibitors / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D013997:Time Factors
D004791:Enzyme Inhibitors; D004798:Enzymes