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Sodium dodecyl sulfate versus acid‐labile surfactant gel electrophoresis: Comparative proteomic studies on rat retina and mouse brain
Author(s) -
König Simone,
Schmidt Oliver,
Rose Karin,
Thanos Solon,
Besselmann Michael,
Zeller Martin
Publication year - 2003
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/elps.200390090
Subject(s) - sodium dodecyl sulfate , pulmonary surfactant , chemistry , proteome , gel electrophoresis , chromatography , electrophoresis , polyacrylamide gel electrophoresis , two dimensional gel electrophoresis , mass spectrometry , biochemistry , gel electrophoresis of proteins , proteomics , gene , enzyme
A long‐chain derivative of 1,3‐dioxolane sodium propyloxy sulfate, with similar denaturing and electrophoretic properties as SDS, and facilitated protein identification following polyacrylamide gel electrophoresis (PAGE) for Coomassie‐stained protein bands, has been tested. Comparative acid‐labile surfactant/sodium dodecyl sulfate two‐dimensional (ALS/SDS 2‐D)‐PAGE experiments of lower abundant proteins from the proteomes of regenerating rat retina and mouse brain show that peptide recovery for mass spectrometry (MS) mapping is significantly enhanced using ALS leading to more successful database searches. ALS may influence some procedures in proteomic analysis such as the determination of protein content and methods need to be adjusted to that effect. The promising results of the use of ALS in bioanalytics call for detailed physicochemical investigations of surfactant properties.