Comparison of SDS-PAGE Protein Profiles of Colorectal Cancer Tissues Extracted Using Three Different Extraction Buffers

Colorectal cancer is one of the major public concerns due to its increasing incidents worldwide. Proteomics approach may serve as a useful tool in understanding the development of the disease. Analysis of protein expression in colorectal cancer and normal tissues will lead to the understanding of the disease that may improve its prognosis. The property of proteins varied dependent on their amino acid composition and folding. Therefore, there is no single extraction buffer possible to extract total proteins from the tissues. In this study, we used three extraction buffers to extract proteins from the homogenized colorectal tissues. The Sodium Oodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SOS-PAGE) profiles of the buffer extracts show common and distinct proteins extracted in each buffer. Excluding the heterogeneous proteins that migrated as multiple bands in SOS-PAGE, five proteins were identified exclusively in the buffers, namely alpha-1-antitrypsin and haptoglobin precursor in Phosphate (Ph) buffer, smooth muscle cell associated protein-1 (SMAP-1b) and keratin 20 in Lysis (Ly) buffer, and actin-gamma 1 (ACTG1) protein in Thiourea (Thio) buffer. The data indicates that the combination of buffers is needed in the proteomic analysis of colorectal tissues.