Competitive adsorption of alpha-lactalbumin and bovine serum albumin to a sulfopropyl ion-exchange membrane.
Breakthrough curves were measured for pure solutions of alpha-lactalbumin (ALA) and bovine serum albumin (BSA) individually, and for a binary mixture of the proteins, using a sulfopropyl ion-exchange membrane. The breakthrough curves were qualitatively consistent with local-equilibrium theory predictions. Competitive adsorption caused displacement of bound BSA monomer by the more strongly binding BSA dimer, illustrating that even apparently single-protein systems may display multicomponent competitive behavior. In the two-protein experiment, ALA was competitively displaced by the more strongly binding BSA monomer and dimer, indicating that the binding strength was in the order: BSA dimer > BSA monomer > ALA.
Weinbrenner
W F
WF
Department of Chemical Engineering, University of Wisconsin, Madison 53706-1619.
Etzel
M R
MR
D000327:Adsorption; D001667:Binding, Competitive; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D007475:Ion Exchange Resins; D007768:Lactalbumin / Q000032:analysis* / Q000737:chemistry; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine / Q000032:analysis* / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet
D007475:Ion Exchange Resins; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine; D007768:Lactalbumin