Effects of tryptic peptide esterification in MALDI mass spectrometry.
Effects of tryptic peptide esterification in MALDI mass spectrometry.
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MALDI 质谱中胰蛋白酶肽酯化的影响。
DOI：
10.1021/ac0481250
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发表时间：
2005
影响因子：
7.4
通讯作者：
Reilly,JamesP
中科院分区：
文献类型：
--
作者：
Kim,Tae-Young;Brun,YvesV;Reilly,JamesP
以不同脂肪链长的醇为原料，考察了酯化反应对MALDI离子产率的影响。对于其电离率随着衍生化而增加的多肽，越疏水的醇往往产生更大的峰增强。从丙醇到甲醇，反应的完备性增加。ASN或Gln侧链上的酰胺基团的不希望的溶解导致意想不到的酯产品。在蛋白质组学实验中，乙醇被认为是酯化反应的最佳乙醇，因为它不需要大量的溶剂分解就可以几乎完全酯化。采用乙醇酯化的方法对凝胶分离蛋白进行了鉴定。
The effect of esterification on MALDI ion yield is investigated by using alcohols having different aliphatic chain lengths. For peptides whose ionization yields increase with derivatization, more hydrophobic alcohols tend to yield greater peak enhancements. The completeness of the reaction increases from propanol to methanol. Undesired solvolysis of the amide group in the side chain of Asn or Gln leads to unexpected ester products. Ethanol is suggested as the optimal alcohol for esterification in proteomics experiments since it yields almost complete esterification without substantial solvolysis. Ethanol esterification was employed to facilitate the identification of gel-separated proteins.