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Comment on “Evidence that the ProPerDP method is inadequate for protein persulfidation detection due to lack of specificity”

机译:评论“证据表明,由于缺乏特异性,对蛋白质过硫化检测的蛋白质脱水检测不充分”

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The recent report by Fan et al . alleged that the ProPerDP method is inadequate for the detection of protein persulfidation. Upon careful evaluation of their work, we conclude that the claim made by Fan et al . is not supported by their data, rather founded in methodological shortcomings. It is understood that the ProPerDP method generates a mixture of cysteine-containing and non–cysteine-containing peptides. Instead, Fan et al . suggested that the detection of non–cysteine-containing peptides indicates nonspecific alkylation at noncysteine residues. However, if true, then such peptides would not be released by reduction and therefore not appear as products in the reported workflow. Moreover, the authors’ biological assessment of ProPerDP using Escherichia coli mutants was based on assumptions that have not been confirmed by other methods. We conclude that Fan et al . did not rigorously assess the method and that ProPerDP remains a reliable approach for analyses of protein per/polysulfidation.
机译:FAN等人最近的报告。据称,适用于检测蛋白质过硫化的方法是不充分的。在仔细评估他们的工作后,我们得出了粉丝等人所制作的索赔。他们的数据不支持他们的数据,相当于方法论缺点。应理解,适当的方法产生含半胱氨酸和含非半胱氨酸肽的混合物。相反,范等人。建议含非半胱氨酸肽的检测表明在非狭窄残留物下的非特异性烷基化。但是,如果是真,那么这种肽不会通过减少释放,因此在报告的工作流程中没有作为产品。此外,使用大肠杆菌突变体对适当DP的作者生物学评估基于其他方法尚未确认的假设。我们得出表示粉丝等人。并未严格评估该方法,并且该方法仍然是分析每种/聚硫化蛋白质的可靠方法。

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