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- W1998963669 abstract "The steady-state rate behaviour of ceruloplasmin in the presence of inhibitory inorganic anions (azide, cyanate, fluoride, chloride and bromide) has been studied in detail. Formation of ternary enzyme · substrate · inhibitor complexes was found to be kinetically insignificant, which most likely indicates that enzyme · substrate complexes are kinetically insignificant also in absence of inhibitors. Equilibrium constants for the inhibitory binding of inorganic anions to oxidized and reduced ceruloplasmin were estimated kinetically (Table 1) in view of a simplified model mechanism described elsewhere. Halogenide ions were found to interact with both oxidized and reduced ceruloplasmin, although inhibition mainly occurs through complex formation with reduced form of the enzyme. Inhibition by azide and cyanate are, similarly, due to strong interactions with a reduced form of ceruloplasmin, whereas complex formation involving oxidized enzyme was found to be kinetically insignificant at low concentrations of inhibitor." @default.
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- W1998963669 date "1972-06-01" @default.
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- W1998963669 title "Inhibition of Ceruloplasmin by Inorganic Anions" @default.
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- W1998963669 doi "https://doi.org/10.1111/j.1432-1033.1972.tb01874.x" @default.
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