Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues.

Abstract

To study the primary structure and regulation of human cholinesterases, oligodeoxynucleotide probes were prepared according to a consensus peptide sequence present in the active site of both human serum pseudocholinesterase (BtChoEase; EC 3.1

Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases

“…Doctor [6][7][8][9][10][11], as have partial sequences of AChEs isolated from human erythrocytes [12,13], human brain [14], and bovine brain [15]. Pharmacological studies and enzyme kinetic studies with these enzymes, including multiple molecular forms, have demonstrated that they possess similar catalytic properties.…”

Cloning, sequencing and functional expression of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti

“…3) is also hydrophilic and interestingly, exhibits complete amino acid identity. This hydrophilic insertion appears to be unique to insect acetylcholinesterases and is absent in both nematode Ace-1 [27] and vertebrate cholinesterase sequences [28][29][30][31][32][33][34][35], lending support to the hypothesis that proteolytic cleavage of the AChE precursor protein could be a common mechanism in insects [25,26]. Boxed residues indicate sequence identity.…”

“…Another conserved feature of the Aedes sequence is the six amino acid consensus sequence FGESAG surrounding the active site serine. This peptide motif is common to all vertebrate [28][29][30][31][32][33][34][35] and invertebrate [24][25][26][27] cholinesterases studied to date. As noted by Hall and Malcolm [25], both the putative signal peptide domain and C-terminus of the insect AChE protein are [25,26] is the hydrophilic region located between Arg-148 and Pro-180 in Drosophila ACHE, where endoproteolytic cleavage of the 75KDa precursor protein into two non-covalently linked polypeptides takes place [37].…”

Promising inhibition of krait snake’s venom acetylcholinesterase by <italic>Salix nigra</italic> and its role as anticancer, antioxidant agent

“…In Asia, most of the deaths are reported due to snake's bite especially of the members of family Elapidae. Family Elapidae's venom contain large amount of acetylcholinesterase (AchE) which causes the acetylcholine's (physiological events controller) inactivation by the enzymatic interruption (Prody et al, 1987;Dave et al, 2000).…”