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- W1984098093 abstract "Irreversible thermal inactivation of the tetrameric form of human plasma butyrylcholinesterase (cholinesterase; EC 3.1.1.8) was studied in water and in deuterium oxide at pH 7 in the temperature range 53–65°C. The enzyme inactivation follows a complex kinetics that may be described by the sum of two apparent first-order processes. The Eyring plot for enzyme inactivation exhibits a wavelike discontinuity over a span of 2 C° around 58°C. This transition was interpreted in terms of equilibrium between two temperature-dependent conformational states. Though2H2O does not alter the overall multistep inactivation process, a slight solvent isotope effect was observed: a stabilizing effect and a shift in the transition temperature. A comparison between several enzyme preparations revealed differences in thermodynamic activation parameters of inactivation suggesting microheterogeneity in enzyme structures. Kinetics of inactivation of usual (E1uE1u) and atypical (E1aE1a) enzymes were compared. The atypical enzyme was found to be more stable than the usual phenotype." @default.
- W1984098093 created "2016-06-24" @default.
- W1984098093 creator A5012524338 @default.
- W1984098093 creator A5015709474 @default.
- W1984098093 date "1988-11-01" @default.
- W1984098093 modified "2023-10-15" @default.
- W1984098093 title "Stability of butyrylcholinesterase: thermal inactivation in water and deuterium oxide" @default.
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- W1984098093 doi "https://doi.org/10.1016/0167-4838(88)90163-x" @default.
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