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Organic ion imaging of biological tissue with secondary ion mass spectrometry and matrix‐assisted laser desorption/ionization
Author(s) -
Todd Peter J.,
Schaaff T. Gregory,
Chaurand Pierre,
Caprioli Richard M.
Publication year - 2001
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.153
Subject(s) - chemistry , mass spectrometry imaging , mass spectrometry , maldi imaging , analytical chemistry (journal) , sample preparation in mass spectrometry , ionization , ion source , sample preparation , direct electron ionization liquid chromatography–mass spectrometry interface , matrix assisted laser desorption/ionization , ion , secondary ion mass spectrometry , ambient ionization , desorption electrospray ionization , protein mass spectrometry , thermal ionization mass spectrometry , mass spectrum , atmospheric pressure laser ionization , matrix (chemical analysis) , electron ionization , chemical ionization , desorption , chromatography , electrospray ionization , organic chemistry , adsorption
Organic secondary ion mass spectrometry (SIMS) and matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry can be used to produce molecular images of samples. This is achieved through ionization from a clearly identified point on a flat sample, and performing a raster of the sample by moving the point of ionization over the sample surface. The unique analytical capabilities of mass spectrometry for mapping a variety of biological samples at the tissue level are discussed. SIMS provides information on the spatial distribution of the elements and low molecular mass compounds as well as molecular structures on these compounds, while MALDI yields spatial information about higher molecular mass compounds, including their distributions in tissues at very low levels, as well as information on the molecular structures of these compounds. Application of these methods to analytical problems requires appropriate instrumentation, sample preparation methodology, and a data presentation usually in a three‐coordinate plot where x and y are physical dimensions of the sample and z is the signal amplitude. The use of imaging mass spectrometry is illustrated with several biological systems. Copyright © 2001 John Wiley & Sons, Ltd.