Open AccessCobra Venom Acetylcholinesterase: Nature of Charge Isoforms
Author(s) -
RABA Raivo,
AAVIKSAAR Aavo
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06900.x
Subject(s) - deamidation , acetylcholinesterase , gene isoform , cobra , chemistry , venom , biochemistry , asparagine , naja , isozyme , aspartic acid , enzyme , snake venom , glutamic acid , stereochemistry , amino acid , computer science , programming language , gene
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.