High Pressure Enzyme Kinetics
The elucidation of the mechanism of enzyme reaction generally requires knowledge of the maximum values of the thermodynamic parameters. High hydrostatic pressure associated with temperature can lead to such data. A description of these approaches is given together with applications where data treatment can be achieved using the general “induced-fit” theory which implies that the binding of substrate to enzyme is a two-step process.
KeywordsEntropy Peroxide Ethyl Enthalpy DMSO
Unable to display preview. Download preview PDF.
- Glasstone, S., Laidler, K.J. and Eyring, H. (1941); The theory of rate processes; McGraw-Hill, New York.Google Scholar
- Balny, C. (1996); Transient enzyme kinetics at high pressure; in High Pressure Effects in Molecular Biophysics and Enzymology, Eds J.L. Markley et al., Oxford Univ. Press.Google Scholar
- Douzou, P. (1977) Cryobiochemistry ( Academic Press, London).Google Scholar
- Balny, C., Hayashi, R., Heremans, K. and Masson, P. (Eds), (1992); High Pressure and Biotechnology, Colloque INSERM, Vol. 224, John Libbey, London.Google Scholar
- Mozhaev, V.V., Heremans, K., Frank, J., Masson, P. and Balny, C. (1994); Exploiting the effects of high hydrostatic pressure in biotechnological applications; 12, 493–501.Google Scholar