PMID: 11342047May 9, 2001Paper

Thermal stability of acetylcholinesterase from Bungarus fasciatus venom as investigated by capillary electrophoresis

Biochimica Et Biophysica Acta
D RochuP Masson

Abstract

Previous studies on the conformation of the monomeric acetylcholinesterase (AChE) from the krait (Bungarus fasciatus) venom showed that the protein possesses a large permanent dipole moment. These studies predicted that thermal irreversible denaturation must occur via partially unfolded states. The thermal stability of Bungarus AChE was determined using capillary electrophoresis (CE) with optimized conditions. Runs performed at convenient temperature scanning rates provided evidence for an irreversible denaturation process according to the Lumry and Eyring model. The mid-transition temperature, T(m), and the effective enthalpy change, DeltaH(m) were determined at different pH. The temperature dependence of the free energy, DeltaG, of Bungarus AChE unfolding was drawn using values of T(m), DeltaH(m) and DeltaC(p) determined by CE. The thermodynamic parameters for the thermal denaturation of the monomeric snake enzyme were compared with those of different dimeric and tetrameric ChEs. It was shown that the changes in the ratio of DeltaH(cal/)DeltaH(vH) and DeltaC(p) reflect the oligomerization state of these proteins. All these results indicate that wild-type monomeric Bungarus AChE is a stable enzyme under standard conditions. Ho...Continue Reading

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Citations

Mar 21, 2002·Biochimica Et Biophysica Acta·Daniel RochuPatrick Masson
Feb 25, 2003·Protein Expression and Purification·Shu-Tao LiuAkio Kato
Mar 29, 2002·Electrophoresis·Ersilia De LorenziGabriele Caccialanza
Feb 5, 2002·Electrophoresis·V Dolnik, K M Hutterer
Aug 30, 2002·European Journal of Biochemistry·Cécile Cléry-BarraudPatrick Masson
Nov 25, 2004·Journal of Chromatography. a·Hui XuHong-Yuan Chen

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