Abstract
The steady-state rate behaviour of human ceruloplasmin in the presence of inhibitory unsaturated or aromatic carboxylic acids has been studied in detail, kinetic data being evaluated and interpreted in view of a simplified model for the action of ceruloplasmin on a mixture of two different reducing substrates. Formation of ternary enzyme · substrate · inhibitor complexes was found to be kinetically insignificant, which is consistent with a competitive inhibition mechanism but more likely indicates that enzyme · substrate complexes are kinetically insignificant also in absence of inhibitors. Binding constants for the interaction between ceruloplasmin and the inhibitors tested appear to be independent of the oxidation-reduction state of the enzyme, indicating that the mechanism of action of unsaturated and aromatic carboxylic acids is distinctly different from that of inhibitory inorganic anions.
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