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 |
|---|---|
| Pages (from-to) | 353-367 |
| Number of pages | 15 |
| Journal | Methods in Enzymology |
| Volume | VOL. 96 |
| State | Published - Dec 1 1983 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
Cite this
Acetylcholinesterase biosynthesis and transport in tissue culture. / Rotundo, Richard L.
In: Methods in Enzymology, Vol. VOL. 96, 01.12.1983, p. 353-367.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Acetylcholinesterase biosynthesis and transport in tissue culture
AU - Rotundo, Richard L
PY - 1983/12/1
Y1 - 1983/12/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020973212&partnerID=8YFLogxK
M3 - Article
C2 - 6361457
AN - SCOPUS:0020973212
VL - VOL. 96
SP - 353
EP - 367
JO - Methods in Enzymology
JF - Methods in Enzymology
SN - 0076-6879
ER -