Vidal_1987_Neurochem.Int_11_135

Homogenization of rat brain with dilute buffer shows that about 15% of the acetylcholinesterase is soluble while the remaining 85% is present in a membrane-bound form which can be brought into solution by extraction with Triton X-100. The effect of temperature on the values of V(max) and K(m) of the buffer-soluble, the membrane-bound and the Triton-soluble forms of acetylcholinesterase have been compared and the results discussed in terms of possible changes in the conformation, dissociation or aggregation of the enzyme molecule. Gradient-gel electrophoresis of the soluble preparations carried out at 4 degrees C or 37 degrees C suggest that the normal tetrameric structure present at 4 degrees C dissociates into monomers and forms some higher molecular weight species at 37 degrees C. The effect of prior storage of the brains in toluene on these properties is also considered.