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Model Proteins

"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. OMICS Group International is one of the leading Open Access Publishers which is publishing 350 scholarly open access journals with the support of 30,000 well-versed scholars as editorial team and aimed to disseminate the scholarly knowledge to the scientific society. OMICS Group also organizing 100 international scientific conferences and events yearly all over the world with the support of 100+ scientific associations worldwide. Citation: Fowler CB, O’LearyTJ, MasonJT (2014) Improving the ProteomicAnalysis of Archival Tissue by Using Pressure-Assisted Protein Extraction:A Mechanistic Approach.J Proteomics Bioinform7: 151-157."
 
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