A Competitive Inhibitor of Tyrosinase
Open Access
- 1 January 1951
- journal article
- research article
- Published by CSIRO Publishing in Australian Journal of Biological Sciences
- Vol. 4 (4), 554-560
- https://doi.org/10.1071/bi9510554
Abstract
The kinetics of the activation of catechol by tyrosinase prepared from the potato and the mushroom, and of its inhibition by Na m-hydroxybenzoate, were studied. The enzyme-substrate dissociation constants differed markedly between the 2 enzyme sources (Ks potato = 5m[image], Ks mushroom = 0.28m[image]), as did also the enzyme-inhibitor dissociation constants (Ki potato = 2.5m[image], Ki mushroom = 0.6m[image]). For both enzyme prepns. Na m-hydroxybenzoate met the requirements of a competitive inhibitor.Keywords
This publication has 5 references indexed in Scilit:
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- A New Method for the Measurement of Tyrosinase Catecholase Activity. II. Catecholase Activity Based on the Initial Reaction VelocityJournal of the American Chemical Society, 1944
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934
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