Abstract
Human serum butyrylcholinesterase (BChE) has been converted into a stable but less active desensitized form when heated at 45°C for 24 h. The desensitized BChE follows Michaelis-Menten kinetics, whereas native enzyme exhibits slightly negative cooperativity with respect to butyrylthiocholine binding. In this study, we investigated the effects of Ni2+, Co2+, and Mn2+ on the desensitized BChE. It is found that all three ions were noncompetitive inhibitors of the desensitized BChE, and K i values have been determined as 7.816±1.060 mM, 48.722±4.635 mM, and 84.795±5.249 mM for Ni2+, Co2+, and Mn2+, respectively. In our previous study, these ions were linear mixed-type inhibitors of the native BChE. This finding confirms that desensitized BChE changes to a different conformation than native BChE. From the comparison of K i values of the trace elements, it can be said that Ni2+ is a more effective inhibitor of the desensitized BChE than Co2+ and Mn2+.
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Cengiz, D., Çokuğraş, A.N. & Tezcan, E.F. Effects of Ni2+, Co2+, and Mn2+ on desensitized butyrylcholinesterase prepared from human serum. Biol Trace Elem Res 93, 55–62 (2003). https://doi.org/10.1385/BTER:93:1-3:55
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DOI: https://doi.org/10.1385/BTER:93:1-3:55