Fractionation of protein mixtures through differential adsorption on a gradient of substituted agaroses of increasing hydrophobicity.
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.
D000588:Amines; D001798:Blood Proteins / Q000032:analysis*; D002021:Buffers; D002846:Chromatography, Affinity / Q000379:methods*; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D012685:Sepharose; D012710:Serum Albumin, Bovine / Q000032:analysis*; D012965:Sodium Chloride; D005719:gamma-Globulins / Q000032:analysis*
D000588:Amines; D001798:Blood Proteins; D002021:Buffers; D008024:Ligands; D005719:gamma-Globulins; D012710:Serum Albumin, Bovine; D012965:Sodium Chloride; D012685:Sepharose