The inactivation of trypsin by heat
- 1 January 1930
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 24 (3) , 606-614
- https://doi.org/10.1042/bj0240606
Abstract
Trypsin was prepared free from enterokinase and the pre-stage of the activator. The course of the heat-inactiyation purified trypsin followed the unimolecular equation. The purified trypsin had an optimum stability at about pH 6.5. The critical increment of the heat-inactivation of trypsin was about 40,000 calories per molar unit of enzyme at pH 5-9.This publication has 2 references indexed in Scilit:
- The Kinetics of Protein DenaturationBiochemical Journal, 1926
- On the ‘heat coagulation’ of proteinsThe Journal of Physiology, 1910