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The trade-offs of this approach are both the increased complexity of peptide digests relative to the original sample and the problem of inferring protein quantitative values from the experimental peptide-centric data [82]. The use of proteolytic enzymes to quantify proteins using IDMS was first proposed in 1996 by Barr et al. [83]. These authors synthesized deuterium-labeled peptides, corresponding to their native counterparts formed by proteolysis, to quantify the apolipoprotein A-1 content of a reference standard, with good precision (CV < 4%). The use of tryptic peptides to quantify proteins requires the selection of peptides ensuring reliability of the quantitative output. These so-called proteotypic peptides should meet several requirements needed for quantitative purposes, which are 1) to be detectable and to provide a good response factor; 2) to be selective of the target protein (unique peptide); and 3) to be chemically stable (i.e. containing no methionine or cysteine). Another property desirable for proteotypic peptides is not to be affected by single amino acid polymorphisms, PTMs, or alternative splicing [85]. Selection of peptides from parts of the protein subject to sequential variability will exclude the quantitative results from all other protein variants. This specificity can be used to quantify the active center of the protein and exclude isoforms of low biological activity from the analysis. 哪位好心人能帮忙翻译一下上述英语句子 |
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