
%0 Journal Article
%A Crewther, WC 
%T The Effect of Ph and Cations on the Thermal Denaturation of Trypsin
%J Australian Journal of Biological Sciences
%D 1953/12/01
%V 6
%N 4
%P 597-616
%K 
%R https://doi.org/10.1071/BI9530597
%U https://www.publish.csiro.au/paper/BI9530597 
%X 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. 
