Phosphoamidase Activity of some Proteolytic Enzymes and Rennin.
- 1 January 1950
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 4 (8) , 1321-1322
- https://doi.org/10.3891/acta.chem.scand.04-1321
Abstract
Phosphoamidase activity (I) of rennin far surpassed that of pepsin and trypsin. (Li, Acta Chem. Scand, 4: 610. 1950). That I of trypsin was not due to an impurity, was apparent since I in the absence of soybean inhibitor was 11.8% and in its presence 1.3%. The authors suggested that initial rennin activity on casein is a splitting of the P-N bonds. The equality of the ratio between coagulating and I in the case of crystalline rennin, pepsin and chymotrypsin supported this view.This publication has 4 references indexed in Scilit:
- The Mode of Action of the Crystalline Pancreatic Proteolytic Enzymes.Chemical Reviews, 1950
- Recherches sur la caséine VI. Sur la transformation de la caséine en paracaséineHelvetica Chimica Acta, 1950
- PHOSPHOPROTEIN PHOSPHATASE IN MAMMALIAN TISSUESJournal of Biological Chemistry, 1949
- The purification and crystallization of renninBiochemical Journal, 1945