GLOBULAR FORMS OF ACETYLCHOLINESTERASE IN CAUDATE NUCLEUS SUPERIOR CERVICAL GANGLIA AND NEUROBLASTOMA CELLS: INTERACTION WITH DETERGENTS

Abstract

Publisher Summary This chapter describes the globular forms of acetylcholinesterase (AChE) in caudate nucleus superior cervical ganglia and neuroblastoma cells. Two classes of AChE molecules have been distinguished: the asymmetric forms in which the catalytic subunits are associated with a collagen-like tail and the globular forms which can exist as monomers (G1), dimers (G2), or tetramers (G4). The globular forms are more complex as they present several variants that differ notably in their solubility and their detergent binding properties. The chspter describes a study in which these properties have been investigated in the case of the globular forms of ox caudate nucleus (CN), ox or rat superior cervical ganglia (SCG), and T28 clone. Homogenization in absence of detergent of the CN, SCG, and T28 cells released, respectively, about 25%, 60%, and 25% of the total activity into a high speed supernatant (H2O soluble AChE). The remaining activity was recovered in a 1% Triton X 100 extract of the aqueous pellets and was referred to as the detergent soluble AChE. The G1 form of CN is almost entirely soluble in absence of detergent, while only a part of this form is present in the H2O soluble AChE of the SCG or T28 cells.