
%0 Journal Article
%A Warner, C 
%T A Competitive Inhibitor of Tyrosinase
%J Australian Journal of Biological Sciences
%D 1951/12/01
%V 4
%N 4
%P 554-560
%K 
%R https://doi.org/10.1071/BI9510554
%U https://www.publish.csiro.au/paper/BI9510554 
%X The kinetics of the activation of catechol by tyrosinase prepared from the potato and the mushroom, and of its inhibition by sodium m-hydroxybenzoate, have been studied. The enzyme-substrate dissociation constants differed markedly between the two enzyme sources (K. potato = 5.OmM, Kg mushroom = O.28mM), as did also the enzyme-inhibitor dissociation constants (K; potato = 2.5mM, Ki mushroom = O.BmM). For both enzyme preparations sodium m-hydroxybenzoate met the requirements of a competitive inhibitor. 
