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- W2000841054 abstract "Monovalent inorganic anions showed an unexpected effect on the inhibition of trehalase (α,α-trehalose glucohydrolase, EC 3.2.1.28) by SH inhibitors. This phenomeon (deinhibition) was caused by monovalent anions, Cl−, Br−, I− and SCN−. F− and CIO4− showed partial deinhibition. Deinhibition was not caused by NO2− and SO4−. The effectiveness of the ‘active anions’ in causing deinhibition was highly dependent on the anion size. Trehalase in the presence of mercuric chloride was ‘activated’ by Cl−, and the activation was saturable. From the results of Dixon plots for trehalase at different concentrations of the ‘activator’ (deinhibitor) and a constant concentration of the substrate, it can be seen that the activator and the inhibitor competed with each other. Thus, it is suggested that the activator and the inhibitor share a common binding site or bind very near each other. The Ki value for mercuric chloride was increased with increasing concentration of NaCl. Therefore, it might be essential to remove the ‘active anions’ in order to determine the inhibitory effect and the Ki value of trehalase for SH inhibitors." @default.
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- W2000841054 date "1982-09-01" @default.
- W2000841054 modified "2023-09-27" @default.
- W2000841054 title "Effect of inorganic anions on the inhibition of trehalase activity by mercuric chloride" @default.
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- W2000841054 doi "https://doi.org/10.1016/0167-4838(82)90403-4" @default.
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