کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1176155 | 961834 | 2008 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A steady state mathematical model for stepwise “slow-binding” reversible enzyme inhibition A steady state mathematical model for stepwise “slow-binding” reversible enzyme inhibition](/preview/png/1176155.png)
The standard mathematical model for stepwise “slow-binding” enzyme inhibition (E+I⇌EI⇌EI∗)(E+I⇌EI⇌EI∗) assumes that the initial enzyme–inhibitor complex EIEI is always at equilibrium with the free component species EE and II. This assumption implies that the dissociation rate constant (EI→E+I)(EI→E+I) is infinitely higher than the isomerization rate constant for EI→EI∗EI→EI∗. This paper presents a more general mathematical treatment, under the steady state approximation rather than the usual rapid-equilibrium approximation, whereby the two rate constants for the disappearance of EIEI are allowed to be comparable in magnitude. Experimentally relevant illustrative examples include discrimination between a single-step and a two-step mechanism for slow-binding inhibition kinetics.
Journal: Analytical Biochemistry - Volume 380, Issue 1, 1 September 2008, Pages 5–12