Ions Modify the Strength of Interaction of Diquat and Paraquat with Some Proteins and Cellulose

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3 Citations (Scopus)

Abstract

The interaction of the bipyridylium herbicides diquat and paraquat with the proteins gliadin and human serum albumin (HSA) as well as with cellulose and the effect of various ions on the strength of interaction were studied by charge-transfer chromatography. Both compound showed very similar behaviour. The ions decreased in each case the strength of interaction, the effect depended nonlinearly on the ion concentration and was of saturation character. Gliadin showed the weakest interaction. HSA binds the bipyridylium compounds in an ion-dependent manner, the strength of interaction is higher than that of cellulose at higher ion concentration. This finding indicates an ion-mediated interaction of unknown character between the bipyridylium herbicides and HSA.

Original languageEnglish
Pages (from-to)428-432
Number of pages5
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume46
Issue number5-6
DOIs
Publication statusPublished - Jun 1 1991

Fingerprint

Diquat
Paraquat
Cellulose
Ions
Serum Albumin
Gliadin
Proteins
Herbicides
Chromatography
Charge transfer

Keywords

  • Bipyridyles
  • Diquat
  • Gliadin
  • Human Serum Albumin
  • Mono- and Divalent Cations
  • Paraquat

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

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abstract = "The interaction of the bipyridylium herbicides diquat and paraquat with the proteins gliadin and human serum albumin (HSA) as well as with cellulose and the effect of various ions on the strength of interaction were studied by charge-transfer chromatography. Both compound showed very similar behaviour. The ions decreased in each case the strength of interaction, the effect depended nonlinearly on the ion concentration and was of saturation character. Gliadin showed the weakest interaction. HSA binds the bipyridylium compounds in an ion-dependent manner, the strength of interaction is higher than that of cellulose at higher ion concentration. This finding indicates an ion-mediated interaction of unknown character between the bipyridylium herbicides and HSA.",
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N2 - The interaction of the bipyridylium herbicides diquat and paraquat with the proteins gliadin and human serum albumin (HSA) as well as with cellulose and the effect of various ions on the strength of interaction were studied by charge-transfer chromatography. Both compound showed very similar behaviour. The ions decreased in each case the strength of interaction, the effect depended nonlinearly on the ion concentration and was of saturation character. Gliadin showed the weakest interaction. HSA binds the bipyridylium compounds in an ion-dependent manner, the strength of interaction is higher than that of cellulose at higher ion concentration. This finding indicates an ion-mediated interaction of unknown character between the bipyridylium herbicides and HSA.

AB - The interaction of the bipyridylium herbicides diquat and paraquat with the proteins gliadin and human serum albumin (HSA) as well as with cellulose and the effect of various ions on the strength of interaction were studied by charge-transfer chromatography. Both compound showed very similar behaviour. The ions decreased in each case the strength of interaction, the effect depended nonlinearly on the ion concentration and was of saturation character. Gliadin showed the weakest interaction. HSA binds the bipyridylium compounds in an ion-dependent manner, the strength of interaction is higher than that of cellulose at higher ion concentration. This finding indicates an ion-mediated interaction of unknown character between the bipyridylium herbicides and HSA.

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