Native Liquid Extraction Surface Analysis Mass Spectrometry: Analysis of Noncovalent Protein Complexes Directly from Dried Substrates

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• 作者：Nicholas J. Martin ; Rian L. Griffiths…
• 关键词：Native mass spectrometry ; Proteins ; Liquid extraction surface analysis ; LESA ; Liquid microjunction sampling ; Direct surface sampling ; Dried blood spots
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2015
• 出版时间：August 2015
• 年：2015
• 卷：26
• 期：8
• 页码：1320-1327
• 全文大小：1,345 KB
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• 作者单位：Nicholas J. Martin (1)
  Rian L. Griffiths (1)
  Rebecca L. Edwards (1) (2)
  Helen J. Cooper (1)
  
  1. School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK
  2. Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA
  
• 刊物主题：Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
• 出版者：Springer US
• ISSN：1879-1123

文摘

Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(αβ)2 4H] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The ‘contact-LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS.