Abstract
Mammalian acetylcholinesterase (AChE) exists in brain as globular tetrameric form (G4 form) of which approximately 80% are amphiphilic membrane bound and about 20% are hydrophilic non-membrane bound enzyme. (for review see Massoulié and Toutant, 1988). The amphiphilic membrane bound G4 form consists of two pairs of catalytic subunits. In one of the two pairs, the catalytic subunits are thought to be linked together by one disulfide bond which is located near the C-terminus. In the other pair, the catalytic subunits are each linked through the same C-terminal disulfide bonds to a structural subunit of approximately 20 kDa in molecular mass which carries the hydrophobic membrane anchor (Gennari et al., 1987; Inestrosa et al., 1987; Roberts et al., 1991; Heider and Brodbeck, 1992). On the other hand, AChE from mammalian erythrocytes consists of two disulfide linked catalytic subunits (G2 form) which are membrane bound through a glycosyl phosphatidylinositol (GPI) moiety covalently attached to the C-terminus of each subunit (for review see Silman and Futerman, 1987).
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Brodbeck, U., Liao, J. (1992). Subunit Assembly and Glycosylation of Mammalian Brain Acetylcholinsterase. In: Shafferman, A., Velan, B. (eds) Multidisciplinary Approaches to Cholinesterase Functions. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3046-6_4
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DOI: https://doi.org/10.1007/978-1-4615-3046-6_4
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