Abstract
Various types of acetylcholinesterase (AChE) subunits are characterized by specific C-terminal peptides. In Torpedo and mammals, alternative exons encode H peptides, which contain a C-terminal signal for glypiation, i. e. cleavage and addition of a glycolipid (GPI) anchor. The H peptides of Torpedo and rat AChE show no homology, except for the presence of cysteines at their N-terminal end, allowing the formation of disulfide-linked dimers, and of a C-terminal hydrophobic region.
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© 1998 Springer Science+Business Media New York
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Bon, S., Coussen, F., Massoulié, J. (1998). The Glycolipid-Addition Signal of Acetylcholinesterase. In: Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. (eds) Structure and Function of Cholinesterases and Related Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1540-5_30
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DOI: https://doi.org/10.1007/978-1-4899-1540-5_30
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