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Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases
Author(s) -
Doctor B.P.,
Chapman T.C.,
Christner C.E.,
Deal C.D.,
De La Hoz D.M.,
Gentry M.K.,
Ogert R.A.,
Rush R.S.,
Smyth K.K.,
Wolfe A.D.
Publication year - 1990
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(90)81522-p
Subject(s) - acetylcholinesterase , sequence (biology) , fetus , chemistry , biochemistry , peptide sequence , cholinesterase , fetal bovine serum , biology , enzyme , endocrinology , pregnancy , genetics , in vitro , gene
The complete amino acid sequence of a mammalian acetylcholinesterase from fetal bovine serum (FBS AChE) is presented. This enzyme has a high degree of sequence identity with other cholinesterases, liver carboxyesterases, esterase‐6, lysophospholipase, and thyroglobulin. The locations of 191 amino acids in 10 regions of the FBS enzyme were compared with corresponding sequences of Torpedo , human, and Drosophila AChEs and human serum butyrylcholinesterase (BChE). In one region there is a marked difference in both the number of amino acids and their sequence between mammalian AChE and other AChEs and the human serum BChE. The amino acid sequence of FBS AChE showed overall homologies of 90% with human AChE, 60% with T. californica AChE, 50% with human serum BChE, and 39% with Drosophila AChE in these regions.