Experiments for Enzyme Kinetic Models

Duration: 37 mins 12 secs
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Description: Atkinson, A
Monday 15 August 2011, 11:45-12:30
 
Created: 2011-08-17 14:05
Collection: Design and Analysis of Experiments
Publisher: Isaac Newton Institute
Copyright: Atkinson, A
Language: eng (English)
Credits:
Author:  Atkinson, A
Director:  Steve Greenham
 
Abstract: Enzymes are biological catalysts that act on substrates. The speed of reaction as a function of substrate concentration typically follows the nonlinear Michaelis-Menten model. The reactions can be modified by the presence of inhibitors, which can act by several different mechanisms, leading to a variety of models, all also nonlinear.

The talk will describe the models and derive optimum experimental designs for model building. When the model is known these include D-optimum designs for all the parameters for which we obtain analytical solutions. Ds-optimum designs for the inhibition constant are also of scientific importance.

When the model is not known, the choice is often between two three-parameter models. These can be combined in a single four-parameter model. Ds-optimum designs for the parameter of combination provide a means of establishing which model is true. However, T-optimum designs for departures from the individual models provide tests of maximum power for departures from the models. With two models on an equal footing, compound T-optimum designs are required. Their properties are compared with those of the Ds-optimum designs in the combined model, which have the advantage of being easier to compute.
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