18O2-Labeling in Quantitative Proteomic Strategies: A Status Report

被引：72
作者：
Fenselau, Catherine [1 ]
Yao, Xudong [2 ]
机构：
[1] Univ Maryland, Dept Chem & Biochem, College Pk, MD 20742 USA
[2] Univ Connecticut, Dept Chem, Storrs, CT 06269 USA
来源：
JOURNAL OF PROTEOME RESEARCH | 2009年 / 8卷 / 05期
关键词：
quantitative proteomics; isotope labeling; clinical proteomics; (18)O-labeling; absolute quantitation; tissue proteomics; plasma proteome; biofilms; mitochondria; plasma membrane; formalin-fixed paraffin; laser capture micro-dissection; affinity fractionation; protein cross-linking; glycoproteins; CATALYZED O-16-TO-O-18 EXCHANGE; MASS-SPECTROMETRY; BACK-EXCHANGE; LC-MS; RELATIVE QUANTIFICATION; MITOCHONDRIAL PROTEINS; INTERNAL STANDARDS; PLASMA-MEMBRANE; SOFTWARE TOOL; ACCURATE MASS;
D O I：
10.1021/pr8009879
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Enzyme-catalyzed (18)O(2)-labeling offers a universal strategy for uniform labeling of all peptides from any kind of proteins, including post-translationally modified proteins. It is applicable to clinical samples with unrivaled sensitivity. This review discusses strengths and limitations, and advocates the separation of proteolysis from the labeling step. Continued advances in software will facilitate widespread use of enzyme-catalyzed (18)O(2)-labeling to determine changes in protein abundances.
引用
收藏
页码：2140 / 2143
页数：4
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