Modulation of acetylcholinesterase activity by glycoside-detergents and their solubilization efficiency for neuronal membranes from bovine nucleus caudatus.

Abstract Several glycoside-detergents were synthesized and tested for solubilization effiency on neuronal membranes. The activity of membrane bound and purified acetylcholinesterase from bovine nucleus caudatus was measured in presence of glycoside-detergents and shown to depend on the length of the alkylchain and the presence of lipid as well. The enzyme activity was not maintained in solutions of octyl-glycoside-detergents, but could be reactivated to a certain extent. This demonstrates the existence of an enzyme-detergent-complex, in which hydrophobic interactions in a region of well defined size must exist for retaining full activity.