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Biophys Rev. 2009 Sep;1(3):131. doi: 10.1007/s12551-009-0015-6. Epub 2009 Sep 09.

Imaging mass spectrometry: principle and application.

Biophysical reviews

Chihiro Murayama, Yoshishige Kimura, Mitsutoshi Setou

Affiliations

  1. Department of Molecular Anatomy, Molecular Imaging Frontier Research Center, Hamamatsu University School of Medicine, 1-20-1 Handayama, Higashi-ku, 431-3192, Hamamatsu, Shizuoka, Japan.
  2. Department of Molecular Anatomy, Molecular Imaging Frontier Research Center, Hamamatsu University School of Medicine, 1-20-1 Handayama, Higashi-ku, 431-3192, Hamamatsu, Shizuoka, Japan. [email protected].

PMID: 28509996 PMCID: PMC5425681 DOI: 10.1007/s12551-009-0015-6

Abstract

Imaging mass spectrometry (IMS) is two-dimensional mass spectrometry to visualize the spatial distribution of biomolecules, which does not need either separation or purification of target molecules, and enables us to monitor not only the identification of unknown molecules but also the localization of numerous molecules simultaneously. Among the ionization techniques, matrix assisted laser desorption/ionization (MALDI) is one of the most generally used for IMS, which allows the analysis of numerous biomolecules ranging over wide molecular weights. Proper selection and preparation of matrix is essential for successful imaging using IMS. Tandem mass spectrometry, which is referred to MS

Keywords: Imaging; Imaging mass spectrometry (IMS); Matrix assisted laser desorption/ionization (MALDI); Principal component analysis (PCA); Time-of-flight mass spectrometer (TOF-MS)

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