Identification of proteome molecules by proteomics using two-dimensional gel electrophoresis and MALDI-TOF MS

Abstract

Genomic technologies have enabled rapid accumulation of information from complex biological systems over the last two decades. The complete DNA sequence is now known for many organisms and the informational database obtained from genome sequencing projects has provided the base for the specification of proteome - the protein complement of genome. Genomic functions can be inferred from the analysis of gene structure and gene expression profiles because proteins are the functional molecules of an organism. Integrated technologies including protein separation, identification, characterization and information manage system are essential to analyze the proteins in complex cellular matrix. This study is focusing on the strategies of proteome analysis using sample preparation, 2-dimensional gel electrophoresis, processing of protein spots and identification of proteins, protein-protein interaction and posttranslational modification using MALDI-TOF-MS. 2-D gel electrophoresis is currently the most powerful protein separation technique and MALDI-TOF MS is powerful identification technique for protein and peptides as a sensitive, rapid, and high resolution analytical method. The developed integrated proteome technologies are very useful to understand the biological phenomena at molecular level by identifying the new molecules and their modifications in various cellular processes, and can be applied for biotechnology including medical science.