Weise C, Kreienkamp H J, Raba R, Aaviksaar A, Hucho F
Freie Universität Berlin, Institut für Biochemie, Federal Republic of Germany.
J Protein Chem. 1990 Feb;9(1):53-7. doi: 10.1007/BF01024984.
About 30% of the primary structure of acetylcholinesterase (AchE) from the cobra Naja naja oxiana has been determined. The sequence around the serine residue labeled by diisopropylfluorophosphate (DFP) was found to be TVTLFGESAGAASVGM which is similar to the active sites of AChE from other tissues. The part of the primary structure determined shows 76% identity with AChE from Torpedo and 42% identity with the Drosophila enzyme. A surprisingly large identity (42% in the sequence determined) was found with lysophospholipase from rat.
眼镜蛇中亚眼镜蛇乙酰胆碱酯酶(AchE)约30%的一级结构已被确定。发现经二异丙基氟磷酸酯(DFP)标记的丝氨酸残基周围的序列为TVTLFGESAGAASVGM,这与来自其他组织的AChE的活性位点相似。所确定的一级结构部分与电鳐的AChE有76%的同源性,与果蝇的酶有42%的同源性。令人惊讶的是,与大鼠溶血磷脂酶有很大的同源性(在所确定的序列中有42%)。