通过测量蛋白版本数量进行的绝对蛋白定量分析，有可能为生物学过程提供重要信息，但除了酿酒酵母的特例外，此前利用标准蛋白质组程序尚未证明这种可能性。
现在，以钩端螺旋体病病原体“肾脏钩端螺旋体”作为第一个目标，一种新的质谱方法被用来确定一个蛋白质组中相当大一部分的绝对蛋白质丰度，而该方法所依据的策略应可普遍应用于很多其他的生物学体系。该研究的结果反映了“肾脏钩端螺旋体”是怎样在总蛋白版本数量保持不变的情况下通过调整蛋白质组的动态平衡来适应环境变化的。（生物谷Bioon.com）
生物谷推荐原始出处：
Nature 460, 762-765 (6 August 2009) | doi:10.1038/nature08184
Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
Johan Malmstr?m1,5, Martin Beck1,5, Alexander Schmidt1,2, Vinzenz Lange1,2, Eric W. Deutsch3 & Ruedi Aebersold1,2,3,4
1 Institute of Molecular Systems Biology, ETH Zurich (Swiss Federal Institute of Technology), Wolfgang Pauli-Strasse 16, CH-8093 Zurich, Switzerland
2 Competence Center for Systems Physiology and Metabolic Diseases, CH-8093 Zurich, Switzerland
3 Institute for Systems Biology, 1441 North 34th Street, Seattle, Washington 98103-8904, USA
4 Faculty of Science, University of Zurich, CH-8057 Zurich, Switzerland
5 These authors contributed equally to this work.
Mass-spectrometry-based methods for relative proteome quantification have broadly affected life science research. However, important research directions, particularly those involving mathematical modelling and simulation of biological processes, also critically depend on absolutely quantitative data—that is, knowledge of the concentration of the expressed proteins as a function of cellular state. Until now, absolute protein concentration measurements of a considerable fraction of the proteome (73%) have only been derived from genetically altered Saccharomyces cerevisiae cells1, a technique that is not directly portable from yeast to other species. Here we present a mass-spectrometry-based strategy to determine the absolute quantity, that is, the average number of protein copies per cell in a cell population, for a large fraction of the proteome in genetically unperturbed cells. Applying the technology to the human pathogen Leptospira interrogans, a spirochete responsible for leptospirosis2, we generated an absolute protein abundance scale for 83% of the mass-spectrometry-detectable proteome, from cells at different states. Taking advantage of the unique cellular dimensions of L. interrogans, we used cryo-electron tomography morphological measurements to verify, at the single-cell level, the average absolute abundance values of selected proteins determined by mass spectrometry on a population of cells. Because the strategy is relatively fast and applicable to any cell type, we expect that it will become a cornerstone of quantitative biology and systems biology.
