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Study of competitive binding of enantiomers to protein by affinity capillary electrochromatography
Ye, ML; Zou, HF; Liu, Z; Wu, RN; Lei, ZD; Ni, JY
KeywordAffinity Capillary Electrochromatography Enantiomers Drug-protein Interaction Bovine Serum Albumin
Source PublicationJOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
2002-01-15
Volume27Issue:3-4Pages:651-660
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences ; Life Sciences & Biomedicine
WOS SubjectChemistry, Analytical ; Pharmacology & Pharmacy
WOS Research AreaChemistry ; Pharmacology & Pharmacy
WOS KeywordBOVINE SERUM-ALBUMIN ; CHROMATOGRAPHY ; SEPARATION ; TECHNOLOGY ; TRYPTOPHAN ; RETENTION
AbstractAffinity capillary electrochromatography (CEC) with zonal elution method was used to probe the competitive interactions of enantiomers with protein. In this approach, a known concentration of a competing agent is continuously applied to a CEC column with bovine serum albumin (BSA) physically adsorbed on SAX packing while injections of a small amount of analyte are made. The binding sites of solutes on the BSA molecule were determined by the changes in the retention factors of the solutes resulted from the addition of competitive agent. By using D- or L-tryptophan as competitive agents and D-, L-tryptophan and benzoin enantiomers as injected analytes showed that BSA molecule has a primary site to strongly bind L-tryptophan, but D-tryptophan dose not bind at this site; D- and L-tryptophan share a weak binding site on the BSA molecule. Benzoin enantiomers do not share any binding sites with either D- or L-tryptophan. Non-chiral compounds of trichloroacetic acid and n-hexanoic acid were applied as the competitive agents to study the binding of warfarin enantiomers to BSA, it was observed that trichloroacetic acid and n-hexanoic acid had a same binding site for warfarin enantiomers binding to BSA molecule. (C) 2002 Elsevier Science B.V. All rights reserved.
Language英语
URL查看原文
WOS IDWOS:000173430500028
Citation statistics
Cited Times:24[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/83223
Collection中国科学院大连化学物理研究所
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Dalian 116011, Peoples R China
Recommended Citation
GB/T 7714
Ye, ML,Zou, HF,Liu, Z,et al. Study of competitive binding of enantiomers to protein by affinity capillary electrochromatography[J]. JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS,2002,27(3-4):651-660.
APA Ye, ML,Zou, HF,Liu, Z,Wu, RN,Lei, ZD,&Ni, JY.(2002).Study of competitive binding of enantiomers to protein by affinity capillary electrochromatography.JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS,27(3-4),651-660.
MLA Ye, ML,et al."Study of competitive binding of enantiomers to protein by affinity capillary electrochromatography".JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS 27.3-4(2002):651-660.
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