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首页> 外文期刊>Analytical chemistry >Quantifying peptides in isotopically labeled protease digests by ion mobility/time-of-flight mass spectrometry
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Quantifying peptides in isotopically labeled protease digests by ion mobility/time-of-flight mass spectrometry

机译:通过离子迁移/飞行时间质谱定量同位素标记的蛋白酶消化物中的肽

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摘要

Ion mobility/time-of-flight techniques have been used to analyze mixtures of isotopically labeled peptides. The isotopic labels were generated by treatment of peptides with N-acetoxysuccinimide (or the deuterated analogue), which results in acetylation (or deuterioacetylation) of the primary amines (i.e., the N-terminus and lysine residues). The relative concentrations of a peptide in each sample are determined by comparing the peak intensities for isotopic pairs. An important consideration is that as mixtures become increasingly complex, isotopic pairs of peaks may overlap with other peaks in the mass spectrum. The influence of the acetyl and deuterioacetyl groups on the mobilities of peptides is considered. The coincidence in mobilities of isotopic pairs provides a means of distinguishing isotopic pairs from other isobaric interferences. [References: 34]
机译:离子迁移率/飞行时间技术已用于分析同位素标记的肽的混合物。同位素标记是通过用N-乙酰氧基琥珀酰亚胺(或氘代类似物)处理肽而产生的,从而导致伯胺的乙酰化(或氘代乙酰化)(即N末端和赖氨酸残基)。通过比较同位素对的峰强度来确定每个样品中肽的相对浓度。一个重要的考虑因素是,随着混合物变得越来越复杂,峰的同位素对可能与质谱中的其他峰重叠。考虑了乙酰基和氘代乙酰基对肽迁移率的影响。同位素对迁移率的一致提供了一种将同位素对与其他同量异位干扰区分开的方法。 [参考:34]

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