Structure specific chromatographic selection in targeted proteomics

被引:21
作者
Mirzaei, H [1 ]
Regnier, F [1 ]
机构
[1] Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2005年 / 817卷 / 01期
关键词
proteomics; amino acid; chromatography; affinity selection; glycosylation; phosphorylation; oxidation; nitration; glycation; specific amino acid selection;
D O I
10.1016/j.jchromb.2004.08.028
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The whole proteome of any organism is too complicated to be analyzed in a simple one-step process and direct attempts for the entire proteome analysis normally lead to considerable loss of information. A practical approach is the targeting of the specific structural feature of interest using chromatography. This approach simplifies the proteome while preserving most of the vital information necessary for analysis. Selection of peptides with specific amino acids (cysteine, histidine and methionine) or N- or C-terminal peptides is an accepted procedure for proteome simplification when general analysis is desired. While selection of enzymatically and non-enzymatically modified proteins and peptides is used when post-translational modifications are targeted. Protein interaction with small molecules as well as other proteins also has been studied using chromatographic selection methods. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:23 / 34
页数:12
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