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Polyproline tetramer organizing peptides in fetal bovine serum acetylcholinesterase

机译:聚脯氨酸四聚体在胎牛中组织肽 血清乙酰胆碱酯酶

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摘要

Acetylcholinesterase (AChE) in the serum of fetal cow is a tetramer. The related enzyme, butyrylcholinesterase (BChE), in the sera of humans and horse requires polyproline peptides for assembly into tetramers. Our goal was to determine whether soluble tetrameric AChE includes tetramer organizing peptides in its structure. Fetal bovine serum AChE was denatured by boiling to release non-covalently bound peptides. Bulk protein was separated from peptides by filtration and by high performance liquid chromatography. Peptide mass and amino acid sequence of the released peptides were determined by MALDI–TOF–TOF and LTQ-Orbitrap mass spectrometry. Twenty polyproline peptides, divided into 5 families, were identified. The longest peptide contained 25 consecutive prolines and no other amino acid. Other polyproline peptides included one nonproline amino acid, for example serine at the C-terminus of 20 prolines. A search of the mammalian proteome database suggested that this assortment of polyproline peptides originated from at least 5 different precursor proteins, none of which were the ColQ or PRiMA of membrane-anchored AChE. To date, AChE and BChE are the only proteins known that include polyproline tetramer organizing peptides in their tetrameric structure.
机译:胎牛血清中的乙酰胆碱酯酶(AChE)是四聚体。人和马血清中的相关酶丁酰胆碱酯酶(BChE)需要聚脯氨酸肽才能组装成四聚体。我们的目标是确定可溶性四聚体AChE是否在其结构中包括四聚体组织肽。通过煮沸使胎牛血清AChE变性,以释放非共价结合的肽。通过过滤和高效液相色谱法从肽中分离出大块蛋白质。通过MALDI-TOF-TOF和LTQ-Orbitrap质谱法测定释放肽的肽质量和氨基酸序列。鉴定了20个多脯氨酸肽,分为5个家族。最长的肽含有25个连续的脯氨酸,不含其他氨基酸。其他多脯氨酸肽包括一个非脯氨酸氨基酸,例如在20个脯氨酸的C-末端的丝氨酸。对哺乳动物蛋白质组数据库的搜索表明,这种多脯氨酸肽的分类来自至少5种不同的前体蛋白,它们都不是膜锚定的AChE的ColQ或PRiMA。迄今为止,AChE和BChE是已知的仅有的在四聚体结构中包括聚脯氨酸四聚体组织肽的蛋白质。

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