Sodium dodecyl sulfate versus acid-labile surfactant gel electrophoresis: comparative proteomic studies on rat retina and mouse brain.
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.
König
Simone
S
Integrated Functional Genomics, Interdisciplinary Clinical Research Center, University of Eye Hospital Münster, University of Münster, Münster, Germany. koenigs@uni-muenster.de
Schmidt
Oliver
O
Rose
Karin
K
Thanos
Solon
S
Besselmann
Michael
M
Zeller
Martin
M
D000143:Acids / Q000737:chemistry*; D000818:Animals; D001921:Brain / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D008297:Male; D013058:Mass Spectrometry; D051379:Mice; D020543:Proteome; D051381:Rats; D017207:Rats, Sprague-Dawley; D012160:Retina / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry
D000143:Acids; D020543:Proteome; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate