2-D Protein Extracts from Drosophila melanogaster

Although the majority of proteins expressed in organisms with relatively low protein complexity, such as Escherichia coli , can be resolved and detected in a single gel (1 ,2 ), this is not true for more complex organisms, such as Drosophila melanogaster . A smaller fraction of the total complement of proteins can be detected in a single gel as the protein complexity of an organism increases. With current detection techniques, this situation can be improved by analyzing subfractions separately and then matching them to each other, preferably using computer-assisted, gel-matching techniques. It has been estimated that about 8% of the proteins encoded by the genome can be analyzed in a single 2-D PAGE of a total protein extract of D. melanogaster (3 ). By matching subfractions, that value can be increased dramatically.