PMID: 3768380Nov 7, 1986Paper

Thermodynamic arguments for temperature-induced cryptic conformational change of human plasma cholinesterase

Biochimica Et Biophysica Acta
P Masson, C Balny

Abstract

The temperature and pressure dependence of the kinetics of the hydrolysis of o-nitrophenylbutyrate by human plasma tetrameric form cholinesterase (EC 3.1.1.8) was studied. The study was carried out on the one hand at atmospheric pressure by spectrophotometry at various temperatures ranging from 0 to 40 degrees C and, on the other hand by high-pressure stopped-flow spectrophotometry at 3.5, 25 and 35 degrees C in the pressure range 10(-3) to 2 kbar. The Arrhenius plot showed a break at 21 +/- 1 degrees C. Kinetic parameters, activation parameters and volume changes are reported. Discontinuities in the thermodynamic quantities obtained from temperature and pressure (up to 0.8 kbar) dependence of hydrolysis rates are discussed; they have been interpreted as the result of a temperature-induced cryptic conformational change of the enzyme at around 20 degrees C. Beyond 1 kbar the kinetics exhibited several complexities: curvature of the progress curves and high positive or negative activation volume changes depending on temperature and substrate concentration. These complex interacting effects between temperature, pressure and substrate concentration are discussed.

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Citations

Dec 1, 1993·Journal of Protein Chemistry·S K Burgess, S L Oxendine
Sep 4, 2012·Chemico-biological Interactions·Marie TrovasletJudith Peters
Mar 8, 2012·Physical Chemistry Chemical Physics : PCCP·Judith PetersMoeava Tehei
Nov 26, 1987·Biochimica Et Biophysica Acta·A Ferro, P Masson
Dec 5, 1990·Biochimica Et Biophysica Acta·P Masson, C Balny
Nov 9, 1989·Biochimica Et Biophysica Acta·C S PayneA D Wolfe
Nov 2, 1988·Biochimica Et Biophysica Acta·P Masson, M Laurentie

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