ENZYME KINETICS A MODERN APPROACH – PART 7 ppsx
ENZYME KINETICS A MODERN APPROACH – PART 7 ppsx
... treatment above assumes that there are no differences in heat capac- ity between native and denatured states of an enzyme and that the heat capacity remains constant throughout the temperature ... stability, enzyme solutions are incubated at a particular temperature and aliquots removed at the appro- priate times. Enzyme activity in these samples is then measured at the enzyme s temp...
Ngày tải lên: 13/08/2014, 07:20
ENZYME KINETICS A MODERN APPROACH – PART 1 pps
... V max /52 3.4 Practical Example / 53 3.5 Determination of Enzyme Catalytic Parameters from the Progress Curve / 58 ENZYME KINETICS A Modern Approach ALEJANDRO G. MARANGONI Department of Food ... new ways of analyzing kinetic data, particularly in the study of pH effects on catalytic activity and multisubstrate enzymes. Since a large proportion of traditional enzyme kinetics...
Ngày tải lên: 13/08/2014, 07:20
ENZYME KINETICS A MODERN APPROACH – PART 2 pptx
... Changes in the reaction rate constant for an acid/base-catalyzed reaction as a function of pH. A negative sloping line (slope =−1) as a function of increasing pH is indicative of an acid-catalyzed ... for example, the reaction A → B → C. Usually, equations in differential or algebraic form are fitted to indi- vidual data sets, A, B, and C and a set of parameter estimates obtained. 2...
Ngày tải lên: 13/08/2014, 07:20
ENZYME KINETICS A MODERN APPROACH – PART 3 pps
... statistic: χ 2 = n i=1 (y i −ˆy i ) 2 s 2 i = n i=1 w i (y i −ˆy i ) 2 (1.125) Consider a typical experiment where the value of a dependent variable is measured several times at a particular value of the independent variable. From these repeated determinations, a mean and variance ... Exact Analytical Solution (Non-Steady-State Approximation) Exact analytical solutions for the rea...
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ENZYME KINETICS A MODERN APPROACH – PART 4 pptx
... is appropriate. When more than two values are compared, a one-way analysis of variance (ANOVA), TABLE 4.2 Rate of Hydration of Fumarate to Malate by Fumarase at various Substrate Concentrations a Velocity ... V ∗ max and K ∗ s correspond, respectively, to apparent enzyme maxi- mum velocity and apparent enzyme substrate dissociation constant at a particular pH. For the model above, V...
Ngày tải lên: 13/08/2014, 07:20
ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
... as v V max = [B] K + [B] (7. 12) where V max = V max [A] K BA + [A] (7. 13) and K = K A s K AB + K AB [A] K BA + [A] = K AB (K A s + [A] ) K BA + [A] (7. 14) From determinations of K and V max at ... complexes EAB (K AB and K BA ), and the enzyme mass balance are, respectively, v = k cat [EAB] (7. 7) K A s = [E] [A] [EA] K B s = [E][B] [EB] (7. 8) K BA = [EB] [...
Ngày tải lên: 13/08/2014, 07:20
ENZYME KINETICS A MODERN APPROACH – PART 6 pptx
... exponential term, and the shape of the curve approaches that of a straight line. Valuable information can be gained from analysis of the early and late stages of this reaction. 11.2.1 Early Stages ... plot for an interfa- cial enzyme. various parameters in Eq. (10.9) on the velocity of a reaction catalyzed by an interfacial enzyme. As the enzyme interface dissociation constant increas...
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ENZYME KINETICS A MODERN APPROACH – PART 8 ppt
... K i of an alter- nate substrate. Addition of an alternate substrate inhibitor to an enzyme assay results in an exponential decrease in rate to some final steady- state turnover of substrate (Fig. ... Finer-Moore, Y. Wataya, and D. V. Santi, Biochemistry 33, 1508 6–1 5094 (1994). Groutas, W. C., R. Kuang, R. Venkataraman, J. B. Epp, S. Ruan, and O. Prakash, Biochemistry 36, 473 9–4 75 0...
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ENZYME KINETICS A MODERN APPROACH – PART 9 docx
... lysine–proline–alanine–glutamic acid–phenylalanine– phenylalanine (NO 2 )–alanine–leucine. c ss2, substrate consisting of the peptide leucine–serine–phenylalanine (NO 2 )–norleucine–leucine– methyl ... than either valine and serine mutants, which had comparable catalytic constants. Compared to valine and serine, alanine has the smallest van der Waals volume and accessible surface area. Theref...
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ENZYME KINETICS A MODERN APPROACH – PART 10 pps
... 4, 5–6 , 20 0–2 02, 203 in characterizing enzyme stability, 14 0–1 46 in modeling irreversible enzyme inhibition, 7 0 7 1, 7 2 7 3, 7 5 7 6, 7 7 7 8 relaxation techniques and, 13 6–1 39 Fit residual analysis, ... enzymes, 14 0–1 57, 20 5–2 12 Standard-state enthalpy of denaturation, 14 7 1 50, 155 Standard-state entropy of denaturation, 14 7 1 50, 155 Standard-state fr...
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