The enzyme acetylcholinesterase consists of a family of molecular forms differing in subunit composition, solubility properties, and subcellular location. The use of a variety of reversible or irreversible active site- directed ligands with different membrane permeability properties permits the selective inactivation of separate pools of enzyme molecules. The application of these inhibitors together with standard biochemical techniques has permitted a detailed characterization of the synthesis and metabolism of the secretory and membrane-bound acetylcholinesterase in tissue-cultured cells. These techniques, with minor modifications and appropriate controls, can also be applied to the study of AChE metabolism in organ culture and in vivo.
ASJC Scopus subject areas
- Molecular Biology