
TY  - JOUR
A1  - Crewther, WC 
T1  - The Effect of Ph and Cations on the Thermal Denaturation of Trypsin
JF  - Australian Journal of Biological Sciences
JO  - Aust. Jnl. Of Bio. Sci.
Y1  - 1953
VL  - 6
IS  - 4
SP  - 597
EP  - 616
KW  - 
UR  - https://doi.org/10.1071/BI9530597 
N2  - Dialysed or very dilute solutions of crystalline trypsin are rapidly and irreversibly inactivated at 40°C. At this temperature and in dilute solution the enzyme is most stable at pH values of about 2.7, 6.6, and 10.7, with intermediate regions of instability. 
ER  -

