Abstract
AbstractThree kinetic rate constants and an initial enzyme concentration are estimated in Britton Chance's classical peroxidase model by applying both the Picard iteration‐orthogonal polynomial and stationary state methods to his transient experimental data. Since this model does not describe the hysteresis exhibited by the data, more complex models are examined in order to account for this behavior. From a study of this hysteresis phenomena which is inherent to the structure of consecutive reactions, it is found that in addition to discriminating between mechanisms much useful information about the history of enzyme induction can be observed from the direction, shape, and area of the hysteresis loop.
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