An amphiphile-dependent form of human brain caudate nucleus acetylcholinesterase: purification and properties

J Neurochem. 1982 Oct;39(4):1050-60. doi: 10.1111/j.1471-4159.1982.tb11496.x.

Abstract

Different forms of acetylcholinesterase (AChE), EC 3.1.1.7, were demonstrated in human brain caudate nucleus. One form was solubilized at high ionic strength, the other with Triton X-100. The detergent-extractable form was purified to homogeneity by affinity chromatography. This form of AChE is amphiphile-dependent; i.e., it was active only in the presence of amphiphiles (detergents or lipids). Further, the enzyme was shown to bind detergents and to interact hydrophobically with Phenyl-Sepharose. In the presence of detergents the enzyme is a tetramer (subunit molecular weight, 78,000) which aggregates on the removal of detergents. Human brain AChE showed a reaction of identity with human erythrocyte AChE in crossed-line immunoelectrophoresis. The high-salt-soluble brain enzyme did not cross-react with the erythrocyte enzyme. The two classes of AChE seem not to be related, as they show no common antigenic determinant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / isolation & purification*
  • Caudate Nucleus / enzymology*
  • Centrifugation, Density Gradient
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoelectrophoresis
  • Isoelectric Focusing
  • Isoenzymes / isolation & purification
  • Kinetics
  • Molecular Weight
  • Octoxynol
  • Polyethylene Glycols

Substances

  • Isoenzymes
  • Polyethylene Glycols
  • Octoxynol
  • Acetylcholinesterase