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Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry
Author(s) -
Chaurand Pierre,
Caprioli Richard M.
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200209)23:18<3125::aid-elps3125>3.0.co;2-#
Subject(s) - mass spectrometry imaging , mass spectrometry , profiling (computer programming) , chemistry , proteomics , computational biology , chromatography , biology , biochemistry , computer science , gene , operating system
Mass spectrometry can be used to map the distribution of targeted compounds in tissue, providing important molecular information in many areas of biological research. Matrix assisted laser desorption/ionization – time of flight – mass spectrometry (MALDI‐TOF‐MS) is well suited for the analysis of tissue samples with a spatial resolution of about 30 νm for compounds in a mass range from 1000 to over 50 000 Da. Direct analysis of tissue sections requires spotting or coating of the tissue with a matrix compound typically sinapinic acid or other cinnamic acid analogs. A raster of this sample by the laser beam and subsequent mass analysis of the desorbed ions can record molecular intensities throughout the section. The overall process is illustrated by profiling and imaging of mouse epididymis sections where protein activity changes markedly throughout the section.