Zeng Rong, Chen Yong-Bing, Shao Xiao-Xia, Shieh Chia-Hui Paul, Miller Ken, Tran Helen, Xia Qi-Chang
Research Center for Proteome Analysis, Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 YueYang Road, Shanghai 200031, China.
Rapid Commun Mass Spectrom. 2003;17(17):1995-2004. doi: 10.1002/rcm.1143.
Digests from ten gel bands containing low abundance proteins were analyzed by both matrix-assisted laser desorption/ionization ion trap (MALDI-IT) and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) methods. MALDI-TOF techniques were able to identify only one protein from all 10 gel bands, while MALDI-IT identified eight proteins from the same 10 bands. The ability to perform MS/MS experiments with a MALDI-IT instrument leads to protein identifications based on both peptide molecular mass and sequence information, and is much less prone to errors and uncertainties introduced by peptide fingerprinting methodologies in which protein identification is based on peptide molecular masses alone.
来自十个含有低丰度蛋白质的凝胶条带的消化产物通过基质辅助激光解吸/电离离子阱（MALDI-IT）和基质辅助激光解吸/电离飞行时间（MALDI-TOF）质谱（MS）方法进行分析。MALDI-TOF技术只能从所有10个凝胶条带中鉴定出一种蛋白质，而MALDI-IT从相同的10个条带中鉴定出了8种蛋白质。使用MALDI-IT仪器进行串联质谱（MS/MS）实验的能力使得能够基于肽分子量和序列信息进行蛋白质鉴定，并且比仅基于肽分子量进行蛋白质鉴定的肽指纹图谱方法所引入的错误和不确定性要少得多。
