Abstract
Conventional procedures of protein purification generallyrely on small differences in the physicochernical properties of proteins in the mixture, e.g. solubility, charge, molecular size and shape. Isolation on the basis of these differences, e.g. by means of ion-exchange chromatography, gelfiltrationo relectrophoresis are often laborious with low yields. This is not surprising considering that the particular proteino finte rest may constitute less than 0.1% of the dry weight of the starting material.