Schipper Raymond, Loof Arnoud, de Groot Jolan, Harthoorn Lucien, van Heerde Waander, Dransfield Eric
Wageningen Centre for Food Sciences, TI Food and Nutrition, Laboratory of Food Chemistry, Wageningen University, the Netherlands.
Ann N Y Acad Sci. 2007 Mar;1098:498-503. doi: 10.1196/annals.1384.010.
In this study, large-scale profiling of salivary proteins and peptides ranging from 2 to 100 kDa was demonstrated using surface-enhanced laser desorption/ionization-time of flight-mass spectrometry (SELDI-TOF-MS). Results show that chip surface type and sample type critically affect the amount and composition of detected salivary proteins. Delayed processing time resulted in both increase and decrease of peak numbers consistent with proteolysis. SELDI-TOF-MS profiles also changed, depending on storage temperature, although sample processing by centrifugation and numbers of freeze-thaw cycles had a minimal impact. In conclusion, SELDI-TOF-MS offers a simple, rapid, high-throughput technique for profiling low-mass (<10 kDa) saliva proteins/peptides. We wish to use this technique to gain insight into the human saliva proteome composition and its changes over time in response to food consumption.
在本研究中，利用表面增强激光解吸/电离飞行时间质谱（SELDI-TOF-MS）对2至100 kDa范围内的唾液蛋白质和肽进行了大规模分析。结果表明，芯片表面类型和样品类型对检测到的唾液蛋白质的数量和组成有至关重要的影响。处理时间延迟导致与蛋白水解一致的峰数量增加和减少。SELDI-TOF-MS谱也因储存温度而改变，尽管通过离心进行的样品处理和冻融循环次数的影响最小。总之，SELDI-TOF-MS为分析低质量（<10 kDa）唾液蛋白质/肽提供了一种简单、快速、高通量的技术。我们希望利用该技术深入了解人类唾液蛋白质组的组成及其随时间因食物摄入而发生的变化。
