DICP OpenIR
学科主题分析化学
Analysis of integral membrane proteome by micro HPLC coupled with MALDI-TOF-MS
Zhao Q(赵群); Sun LL(孙良亮); Wu Q(吴琪); Yuan HM(袁辉明); Liang Z(梁振); Zhang LH(张丽华); Zhang YK(张玉奎)
会议文集7th CNUPO Annual Congress and 3rd International Forum of Proteomics Proteomics and Translational Medicine
会议名称7th CNUPO Annual Congress and 3rd International Forum of Proteomics Proteomics and Translational Medicine
会议日期2011-4-15
2011
会议地点杭州
页码132-0
出版者待补充
出版地待补充
合作性质墙报
部门归属1810
主办者CNHUPO IFP
英文摘要In recent years, matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (MS) was well recognized as a popular technique for analysis of proteome due to its high sensitivity and high throughput1. In our recent work, a high efficient analysis platform combining μRPLC with MALDI-TOF MS was developed for the analysis of integral membrane proteome. In our experiment, bovine serum albumin was firstly adopted as the reference standard protein for optimizing the conditions of MALDI-TOF MS by two layer method2 with a series of matrix recipes including sample to matrix ratios, drop volumes, laser energies and numbers of shots, and it was demonstrated that high quality data of MALDI-TOF MS could be obtained by our optimized protocol, in which 7 mg/mL α-Cyano-4-hydroxycinnamic acid in 0.1% trifluoroacetic acid solution was used as matrix and mixed with equal volume of sample and matrix, laser energy was set to ~40%, 100 shots per single spectrum, accumulating up to 500 shots were utilized for comprehensive identification. With such an optimal MALDI-TOF MS protocol, an integrated approach with combination of peptide separation by μRPLC,automated fraction collection, and detection by MALDI-TOF MS was developed for analysis of the integral membrane proteome from rat brain extracts. By such a method, 61 proteins with p<0.05 were identified, of which about 40 % were integral membrane proteins. All these results indicated that such an approach would provide a promising tool for the large scale membrane proteome analysis.; In recent years, matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (MS) was well recognized as a popular technique for analysis of proteome due to its high sensitivity and high throughput1. In our recent work, a high efficient analysis platform combining μRPLC with MALDI-TOF MS was developed for the analysis of integral membrane proteome. In our experiment, bovine serum albumin was firstly adopted as the reference standard protein for optimizing the conditions of MALDI-TOF MS by two layer method2 with a series of matrix recipes including sample to matrix ratios, drop volumes, laser energies and numbers of shots, and it was demonstrated that high quality data of MALDI-TOF MS could be obtained by our optimized protocol, in which 7 mg/mL α-Cyano-4-hydroxycinnamic acid in 0.1% trifluoroacetic acid solution was used as matrix and mixed with equal volume of sample and matrix, laser energy was set to ~40%, 100 shots per single spectrum, accumulating up to 500 shots were utilized for comprehensive identification. With such an optimal MALDI-TOF MS protocol, an integrated approach with combination of peptide separation by μRPLC,automated fraction collection, and detection by MALDI-TOF MS was developed for analysis of the integral membrane proteome from rat brain extracts. By such a method, 61 proteins with p<0.05 were identified, of which about 40 % were integral membrane proteins. All these results indicated that such an approach would provide a promising tool for the large scale membrane proteome analysis.
语种英语
文献类型会议论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/116014
专题中国科学院大连化学物理研究所
通讯作者Zhang LH(张丽华)
推荐引用方式
GB/T 7714
Zhao Q,Sun LL,Wu Q,et al. Analysis of integral membrane proteome by micro HPLC coupled with MALDI-TOF-MS[C]. 待补充:待补充,2011:132-0.
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