CINETICA ENZIMATICA MICHAELIS MENTEN PDF

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Category:Michaelis–Menten kinetics

Representation of the reversible enzymatic inhibition effect for the kinetic model of Michelis-Menten in transient state. Enzymatic processes that follow the kinetic model of Micahelis-Merten had been studied taking as reference different proposals to describe the reversible inhibition phase. Inhibition proposals were compared based on a generic process. In this process, the kinetic constants received unitary values and the numeric value of the substrate concentration was ten 10 times higher than the numeric value of enzyme concentration.

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Diagrama de Eadie-Hofstee

The most common kind of enzyme kinetics experiment is to vary the concentration of substrate and measure enzyme velocity. The goal is to determine the enzyme's Km substrate concentration that yield a half-maximal velocity and Vmax maximum velocity. If your goal is to determine the turnover number kcat, rather than the Vmax, use an alternative version of the equation. Create an XY data table. Enter substrate concentration into X, and enzyme velocity into Y. If you have several experimental conditions, place the first into column A, the second into column B, etc.

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