title: Cobra venom acetylcholinesterase: nature of charge isoforms.
abstract: Charge isoforms of cobra (Naja naja oxiana) venom acetylcholinesterase, separated by isoelectric focusing, differ only by the number of free carboxyl groups of glutamic and/or aspartic acid side-chains in the enzyme molecule. The isoforms appear to be produced by a post-translational deamidation of accessible glutamin and/or asparagine residues. The isoforms have identical catalytic specificities towards characteristic acetylcholinesterase substrates.
mesh_terms: D000110:Acetylcholinesterase / Q000302:isolation & purification*; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004546:Elapid Venoms / Q000032:analysis*; D004563:Electrochemistry; D007525:Isoelectric Focusing; D010446:Peptide Fragments / Q000302:isolation & purification; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D004546:Elapid Venoms; D010446:Peptide Fragments; D000110:Acetylcholinesterase