Thermal and pH stability of "beta-benzyme".
- 1 February 1987
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 84 (3) , 673-674
- https://doi.org/10.1073/pnas.84.3.673
Abstract
The thermal and pH stability of "beta-benzyme", an artificial chymotrypsin based on beta-cyclodextrin, has been studied and compared with the stability of real chymotrypsin. Artificial chymotrypsin is vastly superior to real chymotrypsin with regard to both temperature and pH stability. The reasons for this increased stability are discussed.This publication has 5 references indexed in Scilit:
- Structure of α-chymotrypsin refined at 1.68 Å resolutionJournal of Molecular Biology, 1985
- Synthesis and evaluation of a miniature organic model of chymotrypsinBiochemical and Biophysical Research Communications, 1985
- Elimination of cannibalistic denaturation by enzyme immobilization or inhibitionProceedings of the National Academy of Sciences, 1981
- Ageing of α-chymotrypsin: Cannibalistic and hydroxide ion reactionsProceedings of the National Academy of Sciences, 1981
- Ultracentrifuge Studies with Absorption Optics. IV. Molecular Weight Determinations at the Microgram Level*Biochemistry, 1966