Effect of salts on the interaction of oxidized glutathione with dibasic amino acids

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Abstract

The interaction of oxidized glutathione (GSSG) with dibasic amino acids was studied with charge-transfer chromatography carried out on unimpregnated cellulose layers in the absence and presence of LiCl, NaCl, KCl, MgCl2 and CaCl2. GSSG decreased in each case the apparent lipophilicity of dibasic amino acids, indicating some type of interaction. Calculations proved that the strength of GSSG dibasic amino acid interaction decreases with increasing concentration of salts suggesting a hydrophilic character of interaction. It can be assumed that electrostatic forces between the carboxyl group of GSSG and the amino groups of amino acids are involved in the interaction. GSSG binds stronger to arginine than to lysine and ornithine suggesting that arginine is probably the primary binding site in proteins for GSSG.

Original languageEnglish
Pages (from-to)739-746
Number of pages8
JournalBiochemistry and Molecular Biology International
Volume44
Issue number4
Publication statusPublished - 1998

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Diamino Amino Acids
Glutathione Disulfide
Salts
Arginine
Magnesium Chloride
Ornithine
Electrostatic force
Chromatography
Static Electricity
Hydrophobic and Hydrophilic Interactions
Cellulose
Lysine
Charge transfer
Binding Sites
Amino Acids

Keywords

  • Dibasic amino acids
  • Hydrophilic interactions
  • Oxidized glutathione

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

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PY - 1998

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AB - The interaction of oxidized glutathione (GSSG) with dibasic amino acids was studied with charge-transfer chromatography carried out on unimpregnated cellulose layers in the absence and presence of LiCl, NaCl, KCl, MgCl2 and CaCl2. GSSG decreased in each case the apparent lipophilicity of dibasic amino acids, indicating some type of interaction. Calculations proved that the strength of GSSG dibasic amino acid interaction decreases with increasing concentration of salts suggesting a hydrophilic character of interaction. It can be assumed that electrostatic forces between the carboxyl group of GSSG and the amino groups of amino acids are involved in the interaction. GSSG binds stronger to arginine than to lysine and ornithine suggesting that arginine is probably the primary binding site in proteins for GSSG.

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