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Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media

文献类型:期刊论文

作者Zhang, Xiaoou2; Samuelsson, Jorgen1; Janson, Jan-Christer1; Wang, Changhai2; Su, Zhiguo3; Gu, Ming3; Fornstedt, Torgny1
刊名JOURNAL OF CHROMATOGRAPHY A
出版日期2010-03-19
卷号1217期号:12页码:1916-1925
关键词Superose 12 10/300 GL Peptides Adsorption isotherms Adsorption energy distribution Heterogeneous interaction Hydrogen bond formation Langmuir model Toth model bi-Langmuir model Mixed mode Electrostatic interactions
ISSN号0021-9673
通讯作者Fornstedt, T
英文摘要The highly cross-linked 12% agarose gel Superose 12 10/300 GL Causes retardation of glycine peptides when mobile phases containing varying concentrations of acetonitrile in water are used An investigation has been made into the retention mechanism behind this retardation using the glycine dipeptide (GG) and tripeptide (GGG) as models The dependence of retention times of analytical-size peaks Under different experimental conditions was interpreted such that the adsorption most probably was caused by the formation of hydrogen bonds but that electrostatic interactions cannot be ruled Out Thereafter, a nonlinear adsorption study Was undertaken at different acetonitrile content in the eluent, using the elution by characteristic points (ECPs) method on strongly overloaded GG and GGG peaks With a new evaluation tool, the adsorption energy distribution (AED) Could be calculated prior to the model selection These calculations revealed that when the acetonitrile content in the eluent was varied from 0% to 20% the interactions turned from (i) being homogenous (GG) or mildly heterogeneous (GGG), (ii) via a more or less stronger degree of heterogeneity around one site to (iii) finally a typical bimodal energy interaction comprising of two sites (GG at 20% and GGG at 10% and 20%) The Langmuir, Toth and bi-Langmuir models described these interesting adsorption trends excellently Thus, the retardation observed for these glycine peptides is interpreted as being of mixed-mode character composed of electrostatic bonds and hydrogen bonds. (C) 2010 Elsevier B.V. All rights reserved
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
类目[WOS]Biochemical Research Methods ; Chemistry, Analytical
研究领域[WOS]Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]ONE-STEP PURIFICATION ; HYDROPHILIC-INTERACTION CHROMATOGRAPHY ; SINGLE-COMPONENT ISOTHERMS ; HOLD-UP TIME ; RETENTION MECHANISM ; THERMODYNAMIC CHARACTERIZATION ; LIQUID-CHROMATOGRAPHY ; ENANTIOMERS ; ELUTION ; DISTRIBUTIONS
收录类别SCI
语种英语
WOS记录号WOS:000275680600008
公开日期2013-11-19
版本出版稿
源URL[http://ir.ipe.ac.cn/handle/122111/6180]  
专题过程工程研究所_生化工程国家重点实验室
作者单位1.Uppsala Univ, Dept Phys & Analyt Chem, Uppsala Biomed Ctr, SE-75124 Uppsala, Sweden
2.Dalian Univ Technol, Dept Biol Sci & Technol, Sch Environm & Biol Sci & Technol, Dalian 116024, Peoples R China
3.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
推荐引用方式
GB/T 7714
Zhang, Xiaoou,Samuelsson, Jorgen,Janson, Jan-Christer,et al. Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media[J]. JOURNAL OF CHROMATOGRAPHY A,2010,1217(12):1916-1925.
APA Zhang, Xiaoou.,Samuelsson, Jorgen.,Janson, Jan-Christer.,Wang, Changhai.,Su, Zhiguo.,...&Fornstedt, Torgny.(2010).Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media.JOURNAL OF CHROMATOGRAPHY A,1217(12),1916-1925.
MLA Zhang, Xiaoou,et al."Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media".JOURNAL OF CHROMATOGRAPHY A 1217.12(2010):1916-1925.

入库方式: OAI收割

来源:过程工程研究所

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