An amphiphile-dependent form of human brain caudate nucleus acetylcholinesterase: purification and properties.
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.
D000110:Acetylcholinesterase / Q000302:isolation & purification*; D002421:Caudate Nucleus / Q000201:enzymology*; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007122:Immunoelectrophoresis; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols
D007527:Isoenzymes; D011092:Polyethylene Glycols; D017830:Octoxynol; D000110:Acetylcholinesterase