|"Model proteins in aqueous solution, our laboratory demonstrated that the majority of protein formaldehyde adducts and cross-links were consistently reversed with mild heating following the removal of excess formaldehyde by dialysis. After fixation in 10% buffered formaldehyde, sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) of 1 mg/ml solutions of RNase A showed a mixture of intermolecular cross-linked proteins composed of monomeric (25%), dimeric (21%), trimeric (18%), tetrameric (15%), pentameric (10%), and hexameric (11%) species (Figure 1, lane 2). Following dialysis, heating the formaldehyde-fixed sample in 20 mM Tris-HCl with 2% SDS at pH 4 resulted in an almost 4-fold increase in monomeric protein.
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Citation: Fowler CB, OâLearyTJ, MasonJT (2014) Improving the ProteomicAnalysis of Archival Tissue by Using Pressure-Assisted Protein Extraction:A Mechanistic Approach.J Proteomics Bioinform7: 151-157."