The effect of temperature on the activity of acetylcholinesterase preparations from rat brain.
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.
Vidal
C J
CJ
Department of Biochemistry, King's College London, Campden Hill, London, W8 7AH, U.K.
Chai
M S
MS
Plummer
D T
DT