Simultaneous Identification of Tyrosine Phosphorylation and Sulfation Sites Utilizing Tyrosine-Specific Bromination

Simultaneous Identification of Tyrosine Phosphorylation and Sulfation Sites Utilizing Tyrosine-Specific Bromination
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利用酪氨酸特异性溴化同时鉴定酪氨酸磷酸化和硫酸化位点

DOI:
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发表时间:
2011
影响因子:
3.2
通讯作者:
Hie
Hie
中科院分区:
化学3区
文献类型:
--
作者:
Jong;Si;Hie

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酪氨酸磷酸化和硫酸盐化在细胞中起着许多关键作用。用磷酸酶或硫酸酶去除磷酸盐或硫酸盐基团,用质谱法测定多肽中的异压磷酸酪氨酸和磺基酪氨酸残留量。在−20℃下与32%的HBr孵育20分钟,得到的酪氨酸残基引入了独特的BR签名。通过对溴化肽的MS/MS分析,可以明确地确定磷酸酪氨酸和硫代酪氨酸的位置。当同一肽中同时含有磷酸酪氨酸、硫代酪氨酸和游离酪氨酸时,可在游离酪氨酸乙酰化后用磷酸酶或硫酸酯酶同时测定。
Tyrosine phosphorylation and sulfation play many key roles in the cell. Isobaric phosphotyrosine and sulfotyrosine residues in peptides were determined by mass spectrometry using phosphatase or sulfatase to remove the phosphate or the sulfate group. Unique Br signature was introduced to the resulting tyrosine residues by incubation with 32% HBr at −20 °C for 20 min. MS/MS analysis of the brominated peptide enabled unambiguous determination of the phosphotyrosine and the sulfotyrosine sites. When phosphotyrosine and sulfotyrosine as well as free tyrosine were present in the same peptide, they could be determined simultaneously using either phosphatase or sulfatase following acetylation of the free tyrosine.
DOI: 10.1021/ac0607764
发表时间: 2006-12-01
影响因子: 7.4
作者:
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通讯作者: Marshall, Alan G.
DOI: 10.1021/pr900044c
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