Analysis of kinetic data for irreversible enzyme inhibition

Analysis of kinetic data for irreversible enzyme inhibition.

Many organophosphorus compounds are irreversible inhibitors of acetylcholinesterase. The methods used in the literature to determine the inhibition kinetic constants usually involve either manual determination of the slope at various points along the inhibition progress curve or fitting polynomials to the curve. The present study investigates the use of non-linear-regression analysis to determi...

Analysis and interpretation of enzyme kinetic data

[email protected] Abstract Analysis of enzyme kinetic data to obtain valid information requires attention to two details that are often given less attention than they need. The first is an experimental design that ensures that the variables treated as independent are truly independent, that different interpretations can be distinguished, and that parameter values can be estimated. The second is ...

Treatment of Enzyme Kinetic Data

The concerted two-state allosteric model proposed by Monod et al. (Monod, J., Wyman, J., and Changeux, J.-P. (1965) J. Mol. Biol. 12, 88-118) is extended to expressions representing the initial velocity as a function of substrate concentration for two-substrate enzymes for which random substrate binding and rapid equilibration of all binding steps prior to a rate-determining conversion in the t...

Comments on the kinetic analysis of enzyme reactions involving an unstable irreversible modifier.

Kinetics of irreversible enzyme inhibition by an unstable inhibitor.

Computer simulations of the irreversible inhibition of an enzyme by an unstable inhibitor are presented. Data obtained at the end point of reaction are shown to conform poorly in many situations with relationships derived from integrated rate equations by setting t = infinity, and the implications concerning the experimental use of this method to determine kinetic constants describing inactivat...