Simultaneous and sequential adsorptions of bovine serum albumin(BSA) and bovine hemoglobin(bHb) was investigated on anion ion-exchange media Q Sepharose FF in batch adsorption experiments to elucidate the mechanism of multi-component protein adsorption.BSA is always preferential adsorbed with bHb inhibited in binary adsorption.Influence on binary adsorption of factors such as pH,salt concentration,initial concentration ratios of proteins and the adsorption sequence are determined.Three models have been tested and compared to describe the competitive binary adsorption of BSA and bHb in all conditions studied.Among the extended Langmuir model gives the best predict of adsorption of the stronger adsorbed protein when its adsorption is not very strong in simultaneous adsorption,the Statistical thermodynamic(ST) model gives the best description of weaker adsorbed protein in simultaneous adsorption,the Steric mass-action(SMA) model is most appropriate multi-component model considering all different conditions for both proteins.
Simultaneous and sequential adsorptions of bovine serum albumin(BSA) and bovine hemoglobin(bHb) was investigated on anion ion-exchange media Q Sepharose FF in batch adsorption experiments to elucidate the mechanism of multi-component protein adsorption.BSA is always preferential adsorbed with bHb inhibited in binary adsorption.Influence on binary adsorption of factors such as pH,salt concentration,initial concentration ratios of proteins and the adsorption sequence are determined.Three models have been tested and compared to describe the competitive binary adsorption of BSA and bHb in all conditions studied.Among the extended Langmuir model gives the best predict of adsorption of the stronger adsorbed protein when its adsorption is not very strong in simultaneous adsorption,the Statistical thermodynamic(ST) model gives the best description of weaker adsorbed protein in simultaneous adsorption,the Steric mass-action(SMA) model is most appropriate multi-component model considering all different conditions for both proteins.