Preparative liquid column chromatography is a powerful method for the
isolation of proteins from complex mixtures. The use of solvent gradie
nts has proved invaluable in the optimisation of the chromatographic s
eparation process. In contrast to isocratic chromatography, the elutin
g strength of the solvent is increased during the separation. To this
end, an increasing proportion of a solvent of high eluting strength is
added to solvent of low eluting strength. This publication is intende
d to contribute to the general understanding of and to a quantitative
description of preparative gradient chromatography of dissolved protei
ns. The analysis is based on the experimental determination of various
chromatograms of the model protein lysozyme on a cation exchanger.