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Mass spectrometric characterization of recombinant and synthetic aggregation-active alpha-Synuclein ((alpha)Syn) polypeptides fragments

机译:重组和合成聚集活性α-突触核蛋白((α)SYN)多肽片段的质谱表征

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1. alpha-Synuclein ((alpha)Syn wt) forms dimeric and oligomeric species as well as N-terminal truncated fragments. 2. N-terminal truncated fragments of (alpha)Syn also form oligomeric structures (gel spot 4, 6, 8 and 10). 3. All spots were successfully eluted from the gel (passive elution) and analyzed by MALDI-TOF-MS. 4. It can be supposed that the formation of (alpha)Syn oligomers is based on the oligomerization of the generated proteolytic fragments.
机译:1.α-突触核蛋白((α)SYN WT)形成二聚体和低聚物质以及N-末端截短的片段。 2. N-末端截短的(α)SYN的碎片也形成低聚结构(凝胶点4,6,8和10)。 3.所有斑点从凝胶(被动洗脱)上成功洗脱,并由MALDI-TOF-MS分析。 4.可以假设(α)SYN低聚物的形成基于所产生的蛋白水解片段的寡聚化。

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