High Resolution Capillary Zone and Gel Electrophoresis of Structurally Similar Amphipatic Glutathione Conjugates Based on Interaction with β-Cyclodextrins
(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:
https://lup.lub.lu.se/record/3516238
- author
- Végvári, Ákos LU ; Larsson, Anna-Karin ; Mannervik, Bengt and Hjertén, Stellan
- publishing date
- 2002
- 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 Inc.
- 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
- 2016-04-04 08:55:12
- date last changed
- 2022-01-29 07:39:41
@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}}, keywords = {{cyclodextrins; electrophoresis; glutathione conjugates; glutathione transferase; peptides}}, language = {{eng}}, number = {{11}}, pages = {{1117--1125}}, publisher = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1002/1439-7633(20021104)3:11<1117::AID-CBIC1117>3.0.CO;2-E}}, volume = {{3}}, year = {{2002}}, }