Abstract
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.
Original language | English (US) |
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Pages (from-to) | 353-367 |
Number of pages | 15 |
Journal | Methods in enzymology |
Volume | 96 |
Issue number | C |
DOIs | |
State | Published - Jan 1 1983 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology