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Protein identification from 2-DE gels by MALDI mass spectrometry

Item Type:Review
Title:Protein identification from 2-DE gels by MALDI mass spectrometry
Creators Name:Jungblut, P. and Thiede, B.
Abstract:Two-dimensional electrophoresis (2-DE) allows the separation of proteins at the level of protein species, which are defined by their chemical structure. Each chemical modification leads to a new protein species. Prerequisites for investigations of protein species are reproducible sample preparation, large gels (20 × 30 cm and larger), high sensitive detection methods, automated evaluation of gels, and sensitive methods for identification of 2-DE-separated protein species. MALDI mass spectrometry with its sensitivity in the fmol range fits with the sensitivity of protein detection on 2-DE gels. Protein mass determination, peptide mass mapping, post-source decay sequencing, and ladder sequencing by MALDI-MS in combination with genome databases have the potential for complete structural investigation on the protein species level. The discrimination of 19 crystalline species of mouse eye lens and of 54 human heart heatshock protein 27 species shows the capacity of the combination of 2-DE with MALDI-MS.
Keywords:Amino Acid Sequence, Crystalline Lens, Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry, Molecular Sequence Data, Myocardium, Peptide Fragments, Two-Dimensional Gel Electrophoresis, Animals, Mice
Source:Mass Spectrometry Reviews
Page Range:145-162
Date:May 1997
Official Publication:https://doi.org/10.1002/(SICI)1098-2787(1997)16:3<145::AID-MAS2>3.0.CO;2-H
PubMed:View item in PubMed

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