Use of an acid-labile surfactant as an SDS substitute for gel electrophoresis and proteomic analysis.

Modern protein identification and analysis relies largely on proteolytic in-gel digestion of proteins separated during polyacrylamide gel electrophoresis (PAGE) followed by mass spectrometric (MS) measurement of the extracted peptides. Sodium dodecyl sulfate (SDS) is routinely used in nonnative PAGE. However, SDS can interfere with MS. We report the use of an acid-labile surfactant (ALS-I) in place of SDS. ALSI is a long chain derivative of 1,3-dioxolane sodium propyloxy sulfate and has similar denaturing and electrophoretic properties as SDS, but it decomposes at low pH and enhances MS detection of proteins.