Abstract
The study of the unfolding process of proteins has been a subject of growing interest during recent years. The availability of recombinant cholinesterases in large amounts permits now to use biophysical tools for gaining information about folding and stability of these enzymes.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Lazar, A., Reuveny, S., Kronman, C., Velan, B. and Shafferman, A. (1993) Cytotechnology, 13, 115–123.
Masson, P. (1995) in High Pressure Chemistry and Physics: A Practical Approach (Isaacs, N.S. Ed), Oxford Univ. Press, in press.
Pace, C.N. (1990) TIBTECH, 8, 93–98
Sanchez-Ruiz, J.M. (1992) Biophys. J., 61, 921–935.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Lebleu, M. et al. (1995). Denaturation of Recombinant Human Acetylcholinesterase. In: Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P. (eds) Enzymes of the Cholinesterase Family. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1051-6_29
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1051-6_29
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1053-0
Online ISBN: 978-1-4899-1051-6
eBook Packages: Springer Book Archive