CRYSTALLINE PEPSIN
Open Access
- 20 July 1931
- journal article
- research article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 14 (6), 713-724
- https://doi.org/10.1085/jgp.14.6.713
Abstract
1. Pepsin solutions which have been completely denatured and inactivated by adjusting to pH 10.5 recover some of their activity when titrated to about pH 5.4 and allowed to stand at 22°C. for 24 to 48 hours. 2. Control experiments show that this inactivation and reactivation are probably not due to the effect of any inhibiting substance. 3. A method of isolation of the reactivated material has been worked out. 4. The reactivated material recovered in this way is a protein with the same general solubility, the same crystalline form, and the same specific proteolytic activity as the original crystalline pepsin. 5. This furnishes additional proof that the proteolytic activity is a property of the protein molecule.This publication has 2 references indexed in Scilit:
- The Reversibility of Protein CoagulationThe Journal of Physical Chemistry, 1931
- CRYSTALLINE PEPSINThe Journal of general physiology, 1930