Matrix-assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF MS)

考古学中心（CfA）是图宾根大学新成立的跨学院核心设施。CfA结合了考古学，地质考古学和应用矿物学工作组的现有仪器和分析能力，以促进蒂宾根大学广泛考古研究范围内的创新，跨学科研究。在过去的十年中，随着古蛋白质组学研究与考古学的日益融合，CfA支持的几个工作组正在寻求分析古代蛋白质，以进一步了解人类的过去。目前，我们没有专门的质谱仪（MS）来完成这项工作，并支付商业价格来分析我们的样品。随着核心设施的建立和雄心勃勃的新项目的追求，我们正在寻求获得基质辅助激光解吸/电离飞行时间质谱仪（MALDI-TOF MS）。MALDI-TOF MS用于分析蛋白质和其他生物分子，包括DNA和碳水化合物。它利用“软电离”，允许脆弱的分子通过MS的真空进行分析。这是通过制备蛋白质与高吸收基质溶液的共结晶实现的。然后，MS用足够能量的激光轰击结晶样品，使肽作为单电荷分子离子通过分析仪，然后由检测器测量。MALDI-TOF MS允许快速测量蛋白质，可选择将多达384个样品点到单个靶板上。因此，MALDI-TOF MS提供了一种高度省时和成本有效的测量蛋白质的方法。MALDI-TOF MS已成为肽质量指纹（PMF）方法的核心，其中蛋白质被提取，酶消化成肽，并进行测量。在古蛋白质组学中，PMF用于靶向胶原蛋白、角蛋白和蛋壳样本，这些样本可以与已发表的参考文库相匹配，以进行分类鉴定。骨、象牙、皮革、兽皮和贝壳等考古文物的工作往往超出了形态学鉴定的范围，PMF成为研究这些物品的宝贵工具。拟议的MALDI-TOF MS将由CfA监督，并设在考古科学研究所（Institut für Naturwissenschaftliche Archäologie：INA）内。虽然该仪器将由核心设施维护，但它对一系列考古项目和工作组将是非常宝贵的。MALDI-TOF MS对高度多样化的考古问题的适用性将使该仪器成为图宾根大学内部和外部几个前沿研究项目的中心。

The Center for Archaeometry (CfA) is a newly established interfaculty core facility at the University of Tübingen. The CfA combines existing instrumentation and analytical competence from the Working Groups for Archaeometry, Geoarchaeology and Applied Mineralogy in order to facilitate innovative, cross-disciplinary research within the broad spectrum of archaeological research conducted at the University of Tübingen. With the growing integration of palaeoproteomic research into archaeological sciences over the past decade, several Working Groups supported by the CfA are seeking to analyse ancient proteins to further our understanding of the human past. At present we have no dedicated mass spectrometer (MS) to achieve this work and pay commercial prices to analyse our samples. With the establishment of the core facility and the pursuit of ambitious new projects, we are seeking to acquire a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF MS). The MALDI-TOF MS is used in the analysis of proteins and other biomolecules, including DNA and carbohydrates. It utilizes ‘soft ionization’ which allows fragile molecules to be analyzed through the vacuum of an MS. This is achieved through the co-crystallization of prepared proteins with a highly absorbing matrix solution. The MS then bombards the crystallized samples with a laser of sufficient energy for the peptides to move through the analyser as singly charged molecular ions which are then measured by a detector. MALDI-TOF MS allows for the rapid measurement of proteins, with the option to spot as many as 384 samples onto a single target plate. MALDI-TOF MS therefore presents a highly time- and cost-efficient means of measuring proteins. The MALDI-TOF MS has become central to peptide mass fingerprinting (PMF) methods, in which proteins are extracted, enzymatically digested into peptides, and measured. In palaeoproteomics, PMF is used to target collagen, keratin, and eggshell specimens that can be matched to published reference libraries for taxonomic identification. Archaeological artefacts of bone, ivory, leather, hide, and shell are often worked beyond the point of morphological identification and PMF becomes an invaluable tool in researching these objects. The proposed MALDI-TOF MS will be overseen by the CfA and housed within the Institute for Archaeological Sciences (Institut für Naturwissenschaftliche Archäologie: INA). While the instrument will be maintained by the core facility it will be invaluable to a range of archaeological projects and Working Groups. The applicability of the MALDI-TOF MS to highly varied archaeological questions will place the instrument at the center of several cutting-edge research projects both internal and external to the University of Tübingen.