Mass spectrometrical identification of brain proteins including highly insoluble and transmembrane proteins

Neurochemistry International
Anna Bierczynska-KrzysikG Lubec

Abstract

Conventional two-dimensional electrophoresis (2DE) is the main technique used for protein profiling of tissues and cells, however separation of strongly acidic, basic or highly insoluble proteins is still limited. A series of methods have been proposed to cope with this problem and the use of discontinuous gel electrophoresis in an acidic buffer system using the cationic detergent benzyldimethyl-n-hexadecylammonium chloride (16-BAC) with subsequent SDS-PAGE followed by mass spectrometry showed that results from 2DE can be complemented by this approach. It was the aim of this study to separate and identify proteins from whole mouse brain that were not demonstrated by 2DE. For this purpose samples were homogenised, soluble proteins were removed by ultracentrifugation and the water-insoluble pellet was resuspended in a mixture containing urea, 16-BAC, glycerol, pyronine Y and dithiothreitol. Electrophoresis was run in the presence of 16-BAC, the strip from the gel containing separated proteins was cut out and was re-run on SDS-PAGE. Protein spots were analyzed by MALDI-TOF-TOF mass spectrometry. One hundred and six individual proteins represented by 187 spots were unambiguously identified consisting of 42 proteins with predicted p...Continue Reading

References

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Citations

Aug 8, 2007·Analytical and Bioanalytical Chemistry·Ralf J BraunMarius Ueffing
Aug 25, 2011·Applied Biochemistry and Biotechnology·Shi-Rou LimLay-Harn Gam
Jun 3, 2008·Biomaterials·Leigh G GriffithsE Christopher Orton
Nov 23, 2006·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Anna Bodzon-KulakowskaJerzy Silberring
Jun 12, 2009·Electrophoresis·Thierry Rabilloud
Apr 4, 2007·Mass Spectrometry Reviews·Anna DrabikJerzy Silberring
Oct 17, 2009·Proteomics·Ingrid MillerElisabetta Gianazza

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