Abstract
Data are presented which indicate the feasibility of protein fractionation at high salt concentrations (greater than or equal to 3 M NaLl) through differential hydrophobic (non-ionic) adsorption on a series of columns of agaroses substituted with ligands of increasing hydrophobicity. By means of such a hydrophobicity gradient of connected columns, separation of mixtures of gamma-globulin and serum albumin, as well as group separation of proteins in dialyzed human blood serum, has been achieved.
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