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Enzyme Kinetics: A Modern Approach by A.G. MARANGONI

By A.G. MARANGONI

Useful Enzyme Kinetics offers a realistic how-to consultant for starting scholars, technicians, and non-specialists for comparing enzyme kinetics utilizing universal software program applications to accomplish effortless enzymatic analyses.

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128) A plot of ln si2 against ln yi yields a straight line with slope = α and yintercept = ln K (Fig. 16). 129) wi = 2 ∼ 2 = yi−α si si ln si2 K is merely a constant that is not included in the calculations, since interest lies in the determination of the relative weighting scheme for a particular data set, not in the absolute values of the weights. If α = 0, si2 is not dependent on the magnitude of the y values, and w = 1/K for all data points. This is the case for an error that is constant throughout the data (homogeneous or constant error).

Some causes for the drop include: 1. The enzyme becomes unstable during the course of the reaction. 2. The degree of saturation of the enzyme by substrate decreases as substrate is depleted. 3. The reverse reaction becomes more predominant as product accumulates. 4. The products of the reaction inhibit the enzyme. 5. Any combination of the factors above cause the drop. It is for these reasons that progress curves for enzyme-catalyzed reactions do not fit standard models for homogeneous chemical reactions, and a different approach is therefore required.

7) Ks κu νu Kt The ratio kcat /Ks (M −1 s−1 ) is the second-order rate constant for the reaction of free enzyme with substrate. The magnitude of this rate constant cannot be greater than the diffusion coefficient of the reactants. , decreased Kt ) until such a diffusion limit is reached for the thermodynamically favored direction of the reaction. Enzyme Kinetics: A Modern Approach. Alejandro G. Marangoni Copyright ¶ 2003 John Wiley & Sons, Inc. 1 PROGRESS CURVE AND DETERMINATION OF REACTION VELOCITY To determine reaction velocities, it is necessary to generate a progress curve.

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