Stability of the Quaternary Structure of Butyrylcholinesterase Subjected to Ultrasound or Hydrostatic Pressure

  • Marie-Thérèse Froment
  • Cécile Cléry
  • Alexandra Weingand-Ziadé
  • Patrick Masson

Abstract

Human butyrylcholinesterase (HuBuChE, EC 3.1.1.8) is a tetrameric enzyme arranged as a dimer of dimers linked by a disulfide bridge at the C-terminus. However, the C-terminal helical segment contains numerous residues presumably involved in the tetramerization domain (1). To evaluate the contribution of aromatic (Ar) residues to tetramerization, the stability of the enzyme tetramer was investigated by hydrostatic pressure and ultrasound techniques. Pressure and ultrasound are known to reinforce Ar-Ar interactions whereas they cause disruption of other weak interations (2).

Keywords

Electrophoresis Disulfide Cholinesterase 

References

  1. 1.
    Blong, R., Bedows, E. and Lockridge, O. Biochem. J. (1997) 327, 747–757.PubMedGoogle Scholar
  2. 2.
    Mozhaev, V., Heremans, K., Frank, J., Masson, P. and Balny, C. Proteins: Struct. Function, and Genet. (1996) 24, 81–91.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Marie-Thérèse Froment
    • 1
  • Cécile Cléry
    • 1
  • Alexandra Weingand-Ziadé
    • 1
  • Patrick Masson
    • 1
  1. 1.Département de Toxicologie -Unité d’EnzymologieCentre de Recherches du Service de Santé des ArméesLa Tronche CedexFrance

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