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Fundamental of Enzyme Kinetics

Basic approaches to solve enzyme kinetics follow  [Pg.334]

System A simplified reaction involving one substrate (uni-substrate enzyme catalysis) for the forward direction as shown by  [Pg.334]

Condition Initial velocities (v) are generally measured at a very low enzyme concentration (i.e. 10 -10 °M) compared with substrate concentrations (A), which are usually greater than 10 M. Thus [Pg.334]

Initial velocity expression Identification of the rate-determining step and description of the initial velocity expression  [Pg.334]

Kinetic treatments Enzyme kinetic data are treated according to two assumptions  [Pg.334]


Copeland, R. A., and Anderson, P. S. (2001) in Textbook of Drug Design and Discovery, 3rd ed., P. Krogsgaard-Larsen, T. Liljefors, and U. Madsen, eds., Taylor and Francis, New York, pp. 328—363. Cornish-Bowden, A. (1995), Fundamentals of Enzyme Kinetics, Portland Press, London. [Pg.47]

Cornish-Bowden, A. Fundamentals of Enzyme Kinetics , Portland Press London, 1995. [Pg.521]

Cornish-Bowden, A. 1999. Fundamentals of enzyme kinetics, Revised Edition. London Portland Press. [Pg.29]

Comish-Bowden, A. (1995) Fundamentals of Enzyme Kinetics. London Portland Press. Fersht, A. (1985) Enzyme Stmcture and Mechanism. Reading W.H.Freeman. [Pg.336]

Cornish-Bowden, A. (1979) Fundamentals of Enzyme Kinetics. Butterworths, London. Costello, S.M., Felix, R.T. and Giese, R.W. (1979) Clin Chem. 25, 1572. [Pg.511]

Cornish-Bowden A (1995) Fundamentals of enzyme kinetics, 2nd edn. Portland Press, London, 344 pp... [Pg.152]

Properties. — A book entitled Fundamentals of Enzyme Kinetics covers all of the enzyme kinetics likely to be required by a student, and provides sufficient additional material to serve as a useful introduction to the subject for research workers coming to biochemistry from other disciplines. The practical aspects of the subject are emphasized and the author discusses methods of purifying... [Pg.418]

Figure 19.9 Interpretation of primary kinetic isotope effects. The bond energy a is shown as a function of R, the bond length. Most molecules are in their lowest vibrational energy state at ordinary temperatures. This state is lower by about 4.8 kj mol in a C-D bond than in a C-H bond. So the C-D bond requires about 4.8 kJ mol more energy to reach the same transition state. Source A Cornish-Bowden, Fundamentals of Enzyme Kinetics, Portland Press, London, 1995. [Pg.354]


See other pages where Fundamental of Enzyme Kinetics is mentioned: [Pg.128]    [Pg.31]    [Pg.10]    [Pg.87]    [Pg.83]    [Pg.333]    [Pg.565]    [Pg.87]    [Pg.1106]   


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