ABSTRACT
No book on the isolation and purification of proteins would be complete without a chapter on protein chromatography. The reason for this is that many proteins of interest occur in very complex environments and their isolation requires a high-resolution method that can exploit even minor differences in structure, such as one amino acid or glycosylation residue, or configuration. Currently, chromatography in its various forms is unsur-passed in this regard. Moreover, since any separation involves at some point the creation of two phases, it is at present difficult to even imagine some other method to replace chromatography with its comparatively “physiological” conditions of temperature and buffer composition and pH in protein separation. Especially in the life sciences, chromatographic separations have become the workhorse for protein separation. In the preparative range there is no other technique of similar performance and in the analytical range only electrophoresis comes close. Moreover, as biotechnology develops as an industry, preparative scale has progressed from the milligram to the gram and kilogram scale. This trend is likely to continue, and other branches of industry may profit from the concomitant progress in preparative chromatographic methods. Examples are plasma fractionation or the dairy industry.
