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Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media
Zhang, Xiaoou2; Samuelsson, Jorgen1; Janson, Jan-Christer1; Wang, Changhai2; Su, Zhiguo3; Gu, Ming3; Fornstedt, Torgny1; Fornstedt, T
2010-03-19
Source PublicationJOURNAL OF CHROMATOGRAPHY A
ISSN0021-9673
Volume1217Issue:12Pages:1916-1925
AbstractThe 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
KeywordSuperose 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
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.chroma.2010.01.058
Indexed BySCI
Language英语
WOS KeywordONE-STEP PURIFICATION ; HYDROPHILIC-INTERACTION CHROMATOGRAPHY ; SINGLE-COMPONENT ISOTHERMS ; HOLD-UP TIME ; RETENTION MECHANISM ; THERMODYNAMIC CHARACTERIZATION ; LIQUID-CHROMATOGRAPHY ; ENANTIOMERS ; ELUTION ; DISTRIBUTIONS
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS IDWOS:000275680600008
Citation statistics
Cited Times:14[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/6180
Collection生化工程国家重点实验室
Corresponding AuthorFornstedt, T
Affiliation1.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
Recommended Citation
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, T.(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.
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