Stepchild phosphohistidine: acid-labile phosphorylation becomes accessible by functional proteomics
Stepchild phosphohistidine: acid-labile phosphorylation becomes accessible by functional proteomics
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DOI：
10.1007/s00216-009-3372-x
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发表时间：
2010-08-01
影响因子：
4.3
通讯作者：
Koenig, Simone
中科院分区：
文献类型：
--
作者：
Hohenester, Ulli Martin;Ludwig, Katrin;Koenig, Simone
生物分析技术优先发展的磷酸羟基氨基酸在过去的调查，有丰富的信息检测丝氨酸，苏氨酸和酪氨酸磷酸化的功能蛋白质组学。然而，对于蛋白质调节和信号传导同样重要的是其他氨基酸如组氨酸的磷酸化，但其检测受到对酸的敏感性的阻碍。质谱结合色谱分析方法使我们能够开始掌握磷组氨酸。P-32标记和磷酸化位点测定的氨基酸分析越来越多地被基于反相肽分离和气相片段化的典型蛋白质组学方法所补充。因此，肽的化学磷酸化是一种有价值的工具，用于生成用于方法开发的分析标准品。
Bioanalytical techniques were preferentially developed for the investigation of phosphohydroxyamino acids in the past and there is a wealth of information on the detection of serine, threonine and tyrosine phosphorylation in functional proteomics. However, similarly important for protein regulation and signalling is the phosphorylation of other amino acids such as histidine, but its detection is hampered by the sensitivity to acid. Mass spectrometry in conjunction with chromatographic methods is allowing us to start to get a handle on phoshohistidine. P-32-labelling and amino acid analysis for phosphorylation site determination is increasingly complemented by typical proteomic approaches based on reversed-phase peptide separation and gas-phase fragmentation. Chemical phosphorylation of peptides is a valuable tool, therefore, for the generation of analytical standards for use in method development.