Proteomic study of muscle sarcoplasmic proteins using AUT-PAGE/SDS-PAGE as two-dimensional gel electrophoresis

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Gianluca PicarielloAldo Di Luccia

Abstract

In the present study, an alternative procedure for two-dimensional (2D) electrophoretic analysis in proteomic investigation of the most represented basic muscle water-soluble proteins is suggested. Our method consists of Acetic acid-Urea-Triton polyacrylamide gel (AUT-PAGE) analysis in the first dimension and standard sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) in the second dimension. Although standard two-dimensional Immobilized pH Gradient-Sodium Dodecyl-Sulphate (2D IPG-SDS) gel electrophoresis has been successfully used to study these proteins, most of the water-soluble proteins are spread on the alkaline part of the 2D map and are poorly focused. Furthermore, the similarity in their molecular weights impairs resolution of the classical approach. The addition of Triton X-100, a non-ionic detergent, into the gel induces a differential electrophoretic mobility of proteins as a result of the formation of mixed micelles between the detergent and the hydrophobic moieties of polypeptides, separating basic proteins with a criterion similar to reversed phase chromatography based on their hydrophobicity. The acid pH induces positive net charges, increasing with the isoelectric point of proteins, thus allowing enhanced res...Continue Reading

Citations

Oct 21, 2011·Journal of Agricultural and Food Chemistry·Phodchanee Phongpa-NganLouise Wicker
Dec 4, 2012·Nutrients·Filomena NazzaroRaffaele Coppola
Aug 17, 2010·Biochimica Et Biophysica Acta·Kay Ohlendieck
Oct 17, 2009·Proteomics·Ingrid MillerElisabetta Gianazza
May 1, 2012·Journal of Proteomics·André Martinho de Almeida, Emøke Bendixen
Dec 3, 2014·Food Chemistry·Aldo Di LucciaGianluca Picariello
Jun 9, 2018·Proteomics·Marta GallegoFidel Toldrá

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