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High‐Resolution Capillary Zone and Gel Electrophoresis of Structurally Similar Amphipathic Glutathione Conjugates Based on Interaction with β ‐Cyclodextrins
Author(s) -
Végvári Ákos,
Larsson AnnaKarin,
Hjertén Stellan,
Mannervik Bengt
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20021104)3:11<1117::aid-cbic1117>3.0.co;2-e
Subject(s) - glutathione , chemistry , capillary electrophoresis , amphiphile , conjugate , tripeptide , cyclodextrin , chromatography , combinatorial chemistry , biochemistry , amino acid , organic chemistry , enzyme , mathematical analysis , mathematics , copolymer , polymer
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 β ‐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 β ‐cyclodextrin to the separation is primarily based on interactions between its hydrophobic cavity and the S ‐alkyl and S ‐benzyl groups of the analytes.