The inactivation of oestrone
- 1 January 1940
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 34 (1), 51-58
- https://doi.org/10.1042/bj0340051
Abstract
Estrone was readily inactivated by H2O2 in alkaline soln. but not in neutral soln.; the methyl ether of estrone was not inactivated by H2O2 in alkaline soln. Estrone, estradiol, and diethylstilboestrol were inactivated by incubation with tyrosinase; a boiled tyrosinase extract had no action. Incubation with catechol oxidase or a combination of catechol oxidase plus catechol did not produce any appreciable in- activation. Complete inactivatioa resulted from the addition of H2O2, but could be prevented by the simultaneous addition of catalase; the addition of catalase did not prevent the inactivation by tyrosinase.This publication has 9 references indexed in Scilit:
- CRYSTALLINE COPPER-PROTEIN POSSESSING TYROSINASE ACTIVITYJournal of the American Chemical Society, 1938
- Animal phenolases and adrenalineBiochemical Journal, 1938
- A comparative study of the production of l-3:4-dihydroxyphenylalanine from tyrosine by tyrosinase from various sourcesBiochemical Journal, 1937
- Metabolism of polycyclic compoundsBiochemical Journal, 1935
- The action of inhibitors on the catechol oxidase of potatoesBiochemical Journal, 1934
- THE AEROBIC OXIDASESPhysiological Reviews, 1928
- The Action of Tyrosinase on PhenolsBiochemical Journal, 1927
- Oxidising EnzymesBiochemical Journal, 1926
- Oxidising EnzymesBiochemical Journal, 1925