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基于基质辅助激光解吸电离(MALDI)的蛋白质组学研究中样品纯化程序的调查。

Investigation of sample-purification procedures for MALDI-based proteomic studies.

作者信息

André Marianne, Karas Michael

机构信息

Institut für Pharmazeutische Chemie, Johann Wolfgang Goethe Universität, Max-von-Laue-Str 9, 60438, Frankfurt, Germany.

出版信息

Anal Bioanal Chem. 2007 Oct;389(4):1047-53. doi: 10.1007/s00216-007-1471-0. Epub 2007 Aug 1.

Abstract

Purification methods for proteomics samples are of crucial concern for improving the quality of the sample delivered to the mass spectrometer. They constitute the link between the mass spectrometer and protein processing and peptide isolation steps that usually require solvents, buffers, or detergents completely incompatible with MS-analysis conditions. This work describes three new clean-up procedures using synthetic membranes and polymer media and compares them with standard procedures. The efficiency of each of the purification procedures was studied via application to four standards and two membrane proteins. This work highlights the importance of versatility in sample preparation, especially for MS-based proteomic investigations.

摘要

蛋白质组学样品的纯化方法对于提高输送到质谱仪的样品质量至关重要。它们构成了质谱仪与蛋白质处理和肽分离步骤之间的联系,而这些步骤通常需要与质谱分析条件完全不兼容的溶剂、缓冲液或去污剂。这项工作描述了三种使用合成膜和聚合物介质的新净化程序,并将它们与标准程序进行了比较。通过应用于四种标准品和两种膜蛋白研究了每种纯化程序的效率。这项工作突出了样品制备中通用性的重要性,特别是对于基于质谱的蛋白质组学研究。

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