Raba R, Aaviksaar A
Eur J Biochem. 1982 Oct;127(3):507-12. doi: 10.1111/j.1432-1033.1982.tb06900.x.
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.
通过等电聚焦分离的眼镜蛇(中亚眼镜蛇)毒液乙酰胆碱酯酶的电荷异构体,仅在酶分子中谷氨酸和/或天冬氨酸侧链的游离羧基数量上有所不同。这些异构体似乎是由可及的谷氨酰胺和/或天冬酰胺残基的翻译后脱酰胺作用产生的。这些异构体对典型的乙酰胆碱酯酶底物具有相同的催化特异性。