Electroelution of Proteins from Polyacrylamide Gels

Abstract

The ability of polyacrylamide gel electrophoresis (PAGE) techniques to resolve the individual components of complex mixtures of several thousand proteins has resulted in this group of methods being one of the most widely used laboratory techniques in biochemistry. Until relatively recently, these techniques were used almost exclusively as analytical tools to characterize proteins in terms of their size, charge, relative hydrophobicity, and abundance. However, the development of a battery of highly sensitive techniques of microchemical characterization, including N-terminal and internal protein sequencing, amino acid compositional analysis, peptide profiling, and mass spectrometry (1,2), has resulted in PAGE often being the method of choice for the micropreparative purification of proteins for subsequent chemical analysis.