期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1157, 期 1-2, 页码 197-206出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2007.05.009
关键词
protein adsorption; beta-lactoglobulin; isocratic elution; gradient elution; hydrophobic interaction chromatography
A two-conformation adsorption model that includes the effects of salt concentration and temperature on both stability and adsorption has been developed to describe the effects of secondary protein unfolding on hydrophobic interaction chromatography (HIC). The model has been applied to a biotech protein and to beta-lactoglobulin on Phenyl Sepharose 6FF low sub HIC media. Thermodynamic property models for adsorption and protein stability with parameters obtained from experimental chromatographic data successfully describe observed chromatographic behavior over ranges of temperature and salt concentration, provide predictions of distribution among different conformers, and give a basis for calculating trends in retention strength and stability with changing conditions, that might prove useful in HIC process development. (c) 2007 Elsevier B.V. All rights reserved.
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