Han Xuemei, Aslanian Aaron, Yates John R
Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrev Pines Road, La Jolla, CA 92037, USA.
Curr Opin Chem Biol. 2008 Oct;12(5):483-90. doi: 10.1016/j.cbpa.2008.07.024.
Mass spectrometry has been widely used to analyze biological samples and has evolved into an indispensable tool for proteomics research. Our desire to understand the proteome has led to new technologies that push the boundary of mass spectrometry capabilities, which in return has allowed mass spectrometry to address an ever-increasing array of biological questions. The recent development of a novel mass spectrometer (Orbitrap) and new dissociation methods such as electron-transfer dissociation has made possible the exciting new areas of proteomic application. Although bottom-up proteomics (analysis of proteolytic peptide mixtures) remains the workhorse for proteomic analysis, middle-down and top-down strategies (analysis of longer peptides and intact proteins, respectively) should allow more complete characterization of protein isoforms and post-translational modifications. Finally, stable isotope labeling strategies have transformed mass spectrometry from merely descriptive to a tool for measuring dynamic changes in protein expression, interaction, and modification.
质谱已被广泛用于分析生物样品，并已发展成为蛋白质组学研究中不可或缺的工具。我们对蛋白质组的理解需求催生了新技术，这些技术推动了质谱分析能力的边界，反过来又使质谱能够解决越来越多的生物学问题。新型质谱仪（轨道阱）和诸如电子转移解离等新的解离方法的最新发展，使得蛋白质组学应用的新领域成为可能。尽管自下而上的蛋白质组学（蛋白水解肽混合物分析）仍然是蛋白质组学分析的主力军，但中而下和自上而下的策略（分别分析较长的肽和完整的蛋白质）应能更全面地表征蛋白质异构体和翻译后修饰。最后，稳定同位素标记策略已将质谱从仅仅具有描述性转变为一种用于测量蛋白质表达、相互作用和修饰动态变化的工具。
