Affinity chromatography of beta-galactosidase on controlled-pore glass derivatives.
Several controlled-pore glass (CPG) derivatives were examined as supports for the affinity chromatographic purification of the enzyme beta-galactosidase. The competitive inhibitor p-aminophenyl-beta-D-thiogalactopyranoside was coupled to an azelaic acid and a malonic acid derivative of 750-A alkylamine CPG of 80-120 mesh and to an azelaic acid derivative of 550-A alkylamine CPG of 40-80 mesh. The latter derivative exhibited particularly good load capacity and separation efficiency; however, both arm lengths were effective. Hydrophobic interactions between the arm and the enzyme contribute to the separation.
D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D003998:Dicarboxylic Acids; D005696:Galactosidases / Q000032:analysis*; D005898:Glass; D006863:Hydrogen-Ion Concentration; D008314:Malonates; D013696:Temperature; D013862:Thiogalactosides
D003998:Dicarboxylic Acids; D008314:Malonates; D013862:Thiogalactosides; D005696:Galactosidases; C010038:azelaic acid