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首页> 外文期刊>Biochemistry >Natural monomeric form of fetal bovine serum acetylcholinesterase lacks the C-terminal tetramerization domain.
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Natural monomeric form of fetal bovine serum acetylcholinesterase lacks the C-terminal tetramerization domain.

机译：胎牛血清乙酰胆碱酯酶的天然单体形式缺乏C端四聚结构域。

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摘要

Acetylcholinesterase isolated from fetal bovine serum (FBS AChE) was previously characterized as a globular tetrameric form. Analysis of purified preparations of FBS AChE by gel permeation chromatography revealed the presence of a stable, catalytically active, monomeric form of this enzyme. The two forms could be distinguished from each other based on their molecular weight, hydrodynamic properties, kinetic properties, thermal stability, and the type of glycans they carry. No differences between the two forms were observed for the binding of classical inhibitors such as edrophonium and propidium or inhibitors that are current or potential drugs for the treatment of Alzheimer's disease such as (-) huperzine A and E2020; tacrine inhibited the monomeric form 2-3-fold more potently than the tetrameric form. Sequencing of peptides obtained from an in-gel tryptic digest of the monomer and tetramer by tandem mass spectrometry indicated that the tetramer consists of 583 amino acid residues corresponding to themature form of the enzyme, whereas the monomer consists of 543-547 amino acid residues. The subunit molecular weight of the protein component of the monomer (major species) was determined to be 59 414 Da and that of the tetramer as 64 239 Da. The N-terminal of the monomer and the tetramer was Glu, suggesting that the monomer is not a result of truncation at the N-terminal. The only differences detected were at the C-terminus. The tetramer yielded the expected C-terminus, CSDL, whereas the C-terminus of the monomer yielded a mixture of peptides, of which LLSATDTLD was the most abundant. These results suggest that monomeric FBS AChE is trimmed at the C-terminus, and the results are consistent with the involvement of C-terminal amino acids in the assembly of monomers into tetramers.
机译：从胎牛血清（FBS AChE）分离的乙酰胆碱酯酶以前被表征为球状四聚体形式。通过凝胶渗透色谱法对纯化的FBS AChE制剂进行分析，发现该酶具有稳定的，催化活性的单体形式。可以根据它们的分子量，流体力学性质，动力学性质，热稳定性和它们携带的聚糖类型来区分这两种形式。两种形式之间的结合没有观察到差异，例如经典的抑制剂（如旋风ium和丙啶）或目前或潜在的用于治疗阿尔茨海默氏病的抑制剂（如石杉碱甲和E2020）的结合。他克林比四聚体形式更有效地抑制单体形式2到3倍。通过串联质谱从单体和四聚体的凝胶内胰蛋白酶消化获得的肽的测序表明，四聚体由对应于酶的酶形式的583个氨基酸残基组成，而单体由543-547个氨基酸残基组成。测定单体（主要种类）的蛋白质组分的亚单位分子量为59 414 Da，四聚体的亚单位分子量为64 239 Da。单体和四聚体的N末端为Glu，表明该单体不是N末端被截短的结果。检测到的唯一差异是在C端。四聚体产生预期的C末端CSDL，而单体的C末端产生肽的混合物，其中LLSATDTLD最丰富。这些结果表明，单体FBS AChE在C末端被修整，其结果与C末端氨基酸参与单体组装成四聚体的过程是一致的。

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