Effect of Structural Properties of Both Proteins and Stationary Phases to Adsorption Behavior of Proteins in Hydrophobic Interaction Chromatography
A series of specially designed agarose-based HICadsorbents were examined using human immunoglobulin G(IgG) and human serum albumin (HSA) as model proteins, toinvestigate the effects of structural properties of both proteinsand stationary phases on the adsorption behavior in HIC. Theadsorbents examined differ from each other in terms of liganddensity, spacer arm and ligand type. Dynamic binding capacity(DBC) was determined to reflect the retention of proteins onadsorbents. The results showed that the adsorption behaviors ofIgG and HSA on hydrophobic adsorbents were in differentmanner. HSA tended to be retained in a HIC adsorbent with highlocal hydrophobicity within a small area, and their interactionwas strictly salt-dependent; whereas IgG was sensitive to spatialaccessibility of hydrophobic ligands rather than ligand type. Thismanner of adsorption enabled IgG to be adsorbed on adsorbentswith relatively high ligand density in absence of water-structuringsalt. The results were ascribed to the differentstructural flexibility, hydrophobic surface distribution and size ofIgG and HSA, two proteins with different types of structure.
Jun Ren Zhiqian Pi Xue Lin Li Xu Jian Xie Lingyun Jia
Department of Bioscience and Biotechnology Dalian University of Technology Dalian, China
国际会议
成都
英文
1-5
2010-06-18（万方平台首次上网日期，不代表论文的发表时间）