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.
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