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High Resolution Capillary Zone and Gel Electrophoresis of Structurally Similar Amphipatic Glutathione Conjugates Based on Interaction with β-Cyclodextrins

Végvári, Ákos LU ; Larsson, Anna-Karin; Mannervik, Bengt and Hjertén, Stellan (2002) In ChemBioChem 3(11). p.1117-1125
Abstract
The tripeptide glutathione is a prominent intracellular constituent that provides protection against genotoxic and carcinogenic electrophiles and is also a component of several biological signal substances. Glutathione conjugates, free glutathione, and glutathione disulfide contain charged amino acid residues, which contribute to solubility in aqueous media.However , the amphipathic nature of glutathione conjugates and the small differences that may distinguish the S substituents, pose analytical problems in their resolution.The present study demonstrates how homologous S-alkyl and S-benzyl conjugates of high structural similarity can be

efficiently resolved by capillary electrophoresis.Inclusion of b-cyclodextrins in the buffer... (More)
The tripeptide glutathione is a prominent intracellular constituent that provides protection against genotoxic and carcinogenic electrophiles and is also a component of several biological signal substances. Glutathione conjugates, free glutathione, and glutathione disulfide contain charged amino acid residues, which contribute to solubility in aqueous media.However , the amphipathic nature of glutathione conjugates and the small differences that may distinguish the S substituents, pose analytical problems in their resolution.The present study demonstrates how homologous S-alkyl and S-benzyl conjugates of high structural similarity can be

efficiently resolved by capillary electrophoresis.Inclusion of b-cyclodextrins in the buffer or in a polyacrylamide gel affords baseline separation of the analytes.The separation methods described are applicable to enzyme assays in vitro and to the identification and quantification of glutathione conjugates of

importance in toxicology and physiology.The contribution of b-cyclodextrin to the separation is primarily based on interactions between its hydrophobic cavity and the S-alkyl and S-benzyl groups of the analytes. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cyclodextrins, electrophoresis, glutathione conjugates, glutathione transferase, peptides
in
ChemBioChem
volume
3
issue
11
pages
1117 - 1125
publisher
John Wiley & Sons
external identifiers
  • scopus:0037021353
ISSN
1439-4227
DOI
10.1002/1439-7633(20021104)3:11<1117::AID-CBIC1117>3.0.CO;2-E
language
English
LU publication?
no
id
932200e7-3578-4cf2-ada3-423701261d94 (old id 3516238)
date added to LUP
2013-02-25 10:53:01
date last changed
2017-01-01 07:40:22
@article{932200e7-3578-4cf2-ada3-423701261d94,
  abstract     = {The tripeptide glutathione is a prominent intracellular constituent that provides protection against genotoxic and carcinogenic electrophiles and is also a component of several biological signal substances. Glutathione conjugates, free glutathione, and glutathione disulfide contain charged amino acid residues, which contribute to solubility in aqueous media.However , the amphipathic nature of glutathione conjugates and the small differences that may distinguish the S substituents, pose analytical problems in their resolution.The present study demonstrates how homologous S-alkyl and S-benzyl conjugates of high structural similarity can be<br/><br>
efficiently resolved by capillary electrophoresis.Inclusion of b-cyclodextrins in the buffer or in a polyacrylamide gel affords baseline separation of the analytes.The separation methods described are applicable to enzyme assays in vitro and to the identification and quantification of glutathione conjugates of<br/><br>
importance in toxicology and physiology.The contribution of b-cyclodextrin to the separation is primarily based on interactions between its hydrophobic cavity and the S-alkyl and S-benzyl groups of the analytes.},
  author       = {Végvári, Ákos and Larsson, Anna-Karin and Mannervik, Bengt and Hjertén, Stellan},
  issn         = {1439-4227},
  keyword      = {cyclodextrins,electrophoresis,glutathione conjugates,glutathione transferase,peptides},
  language     = {eng},
  number       = {11},
  pages        = {1117--1125},
  publisher    = {John Wiley & Sons},
  series       = {ChemBioChem},
  title        = {High Resolution Capillary Zone and Gel Electrophoresis of Structurally Similar Amphipatic Glutathione Conjugates Based on Interaction with β-Cyclodextrins},
  url          = {http://dx.doi.org/10.1002/1439-7633(20021104)3:11<1117::AID-CBIC1117>3.0.CO;2-E},
  volume       = {3},
  year         = {2002},
}