The activation phenomena of papain and cathepsin
- 1 January 1935
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 29 (1), 13-20
- https://doi.org/10.1042/bj0290013
Abstract
Vit. C -Fe", pyruvic acid -Fe", and succinic acid -Fe" indirectly produced on unpurified papain (but not in purified, inactivated papain) an activation de-pendng on the reduction of fixed S-S proteins to the SH form. When S-S proteins were added to it, the above-named complexes activated purified papain. Similar results were obtained with cathepsin. Papain and cathepsin in the active state were probably SH proteins; in the reversibly inactivated forms, they appeared to be S-S proteins. The real activators were sulfhydryl compounds.This publication has 3 references indexed in Scilit:
- The relation of intermediary metabolic products to arginase activationBiochemical Journal, 1934
- The influence of vitamin C on intracellular enzyme actionBiochemical Journal, 1933
- The reduction of nitrates in animal tissuesBiochemical Journal, 1928