Interaction of Synthetic Proanthocyanidin Dimer and Trimer with Bovine Serum Albumin and Purified Bean Globulin Fraction G-l

William E. Artz, Paul D. Bishop, A. Keith Dunker, Edward G. Schanus, Barry G. Swanson

Research output: Contribution to journalArticle

68 Scopus citations

Abstract

To evaluate the type of binding involved, thermodynamic analysis of the temperature dependence of proanthocyanidin binding to bovine serum albumin (BSA) and bean glycoprotein G-l (G-l) was investigated. Binding was analyzed with tritiated proanthocyanidin by ultrafiltration to separate free ligand and protein-bound ligand. Binding constants were determined from Scatchard plots. Van't Hoff plots indicated proanthocyanidin binding to BSA was spontaneous and entropy driven. Analysis with cis-parinaric acid supported the conclusion drawn from the thermodynamic analysis that the binding of proanthocyanidin to BSA was a hydrophobic interaction. Van't Hoff plots indicated proanthocyanidin binding to native G-l protein was also spontaneous but, in contrast to BSA, enthalpy driven. Analysis with cis-parinaric acid confirmed the hydrophilic character of proanthocyanidin binding to native G-l. Evaluation of proanthocyanidin binding to heat-denatured G-l with cis-parinaric acid indicated hydrophobic interactions.

Original languageEnglish (US)
Pages (from-to)417-421
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume35
Issue number3
DOIs
StatePublished - May 1 1987
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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