Studies on the reversible inactivation of papain and cathepsin
- 1 January 1935
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 29 (1) , 5-12
- https://doi.org/10.1042/bj0290005
Abstract
Commercial papain was inactivated by treatment with alloxan, methylglyoxal, H2O2, and by the system, xanthine oxidase + hypoxanthine + peroxidase. Cathepsin was inactivated by alloxan and methylglyoxal. The loss of activity paralleled the loss of SH; the activity could be restored by addition of cysteine or H2S. Cathepsin inactivated by iodoacetic acid could not be reactivated by direct addition of cysteine or H2S. The preparation of large quantities of reversibly inactivated papain and cathepsin is descr.This publication has 4 references indexed in Scilit:
- The influence of vitamin C on intracellular enzyme actionBiochemical Journal, 1933
- Milk peroxidaseBiochemical Journal, 1932
- Studies on Xanthine OxidaseBiochemical Journal, 1925
- Studies on Xanthine OxidaseBiochemical Journal, 1924