The purification and crystallization of rennin
- 1 January 1945
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 39 (2), 179-186
- https://doi.org/10.1042/bj0390179
Abstract
The crystallization of rennin was described and evidence for the purity of the crystals presented. Rennin crystals possessed a low solubility in water and were dried without decomposition. Rennin was believed to be a protease, acting optimally on Hb at pH 3.7.This publication has 4 references indexed in Scilit:
- The total nitrogen content of egg albumin and other proteinsBiochemical Journal, 1943
- Pure Crystalline RenninNature, 1943
- THE CRITERIA OF PURITY USED IN THE STUDY OF LARGE MOLECULES OF BIOLOGICAL ORIGINBiological Reviews, 1940
- THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBINThe Journal of general physiology, 1938