NDLI: Effect of Structural Properties of Both Proteins and Stationary Phases to Adsorption Behavior of Proteins in Hydrophobic Interaction Chromatography

Content Provider	IEEE Xplore Digital Library
Author	Jun Ren Zhiqian Pi Xue Lin Li Xu Jian Xie Lingyun Jia
Copyright Year	2010
Abstract	A series of specially designed agarose-based HIC adsorbents were examined using human immunoglobulin G (IgG) and human serum albumin (HSA) as model proteins, to investigate the effects of structural properties of both proteins and stationary phases on the adsorption behavior in HIC. The adsorbents examined differ from each other in terms of ligand density, spacer arm and ligand type. Dynamic binding capacity (DBC) was determined to reflect the retention of proteins on adsorbents. The results showed that the adsorption behaviors of IgG and HSA on hydrophobic adsorbents were in different manner. HSA tended to be retained in a HIC adsorbent with high local hydrophobicity within a small area, and their interaction was strictly salt-dependent; whereas IgG was sensitive to spatial accessibility of hydrophobic ligands rather than ligand type. This manner of adsorption enabled IgG to be adsorbed on adsorbents with relatively high ligand density in absence of water-structuring salt. The results were ascribed to the different structural flexibility, hydrophobic surface distribution and size of IgG and HSA, two proteins with different types of structure.
Starting Page	1
Ending Page	5
File Size	282155
Page Count	5
File Format	PDF
ISBN	9781424447121
ISSN	21517622
DOI	10.1109/ICBBE.2010.5517033
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2010-06-18
Publisher Place	China
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subject Keyword	Protein engineering Biotechnology Purification Laboratories Humans Ash Amino acids Separation processes Physics Immune system
Content Type	Text
Resource Type	Article

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