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Identical N‐terminal peptide sequences of asymmetric forms and of low‐salt‐soluble and detergent‐soluble amphiphilic dimers of Torpedo acetylcholinesterase
Author(s) -
Bon Suzanne,
Chang Jui-Yoa,
Strosberg A.Donny
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81112-7
Subject(s) - torpedo , amphiphile , peptide , acetylcholinesterase , chemistry , salt (chemistry) , terminal (telecommunication) , biochemistry , enzyme , organic chemistry , copolymer , receptor , acetylcholine receptor , polymer , telecommunications , computer science
We have determined partial N‐terminal sequences of acetylcholinesterase (AChE) catalytic subnunits from Torpedomarmorata electric organs and from bovine caudate nucleus. We obtain identical sequences (23 amino acids) for the soluble (‘low‐salt‐soluble’ or LSS fraction) and particulate (‘detergent‐soluble’, or DS fraction) amphiphilic dimers (G 2 form) and for the asymmetric, collagen‐tailed forms (‘high‐salt‐soluble’, or HSS fraction, A 12 + A 8 forms). There are two amino acid differences, at position 3 (Asp/His) and 20 (Ile/Val), with the sequences obtained for T . californica by MacPhee‐Quigley et al. [(1985) J. Biol. Chem. 260, 12185‐12189] for the soluble G 2 form and the lytic G 4 form which is derived from asymmetric AChE. The bovine sequence (12 amino acids) presents an identity of 4 amino acids (Glu‐Leu‐Leu‐Val) with that of Torpedo , at positions 5–8 ( Torpedo ) and 7–10 (bovine). There is also a clear homology with the sequence of human butyrylcholinesterase [(1986) Lockridge et al. J. Biol. Chem., in press] indicating that these enzymes probably derive from a common ancestor.