CRYSTALLINE PEPSIN
Open Access
- 20 September 1932
- journal article
- research article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 16 (1) , 33-40
- https://doi.org/10.1085/jgp.16.1.33
Abstract
The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45°C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate that none of the split products of the protein molecule possess any appreciable activity compared to that of the original protein.This publication has 4 references indexed in Scilit:
- PEPSIN ACTIVITY UNITS AND METHODS FOR DETERMINING PEPTIC ACTIVITYThe Journal of general physiology, 1932
- CRYSTALLINE PEPSINThe Journal of general physiology, 1931
- CRYSTALLINE PEPSINThe Journal of general physiology, 1930
- PROTEIN COAGULATION AND ITS REVERSALThe Journal of general physiology, 1929