Fluorescence anisotropy analysis of protein-antibody interaction

Nadia Barbero, Lucia Napione, Pierluigi Quagliotto, Simona Pavan, Claudia Barolo, Ermanno Barni, Federico Bussolino, Guido Viscardi

Research output: Contribution to journalArticlepeer-review


The interaction between glutathione S-transferase and its antibody α-glutathione S-transferase (B-14) was studied using fluorescence anisotropy, subsequent to glutathione S-transferase bioconjugation with fluorescein-5-maleimide, leading to the determination of the dissociation and association binding constants, Kd and Ka; good binding specificity was observed between glutathione S-transferase and the antibody B-14. The use of spectroscopic techniques, fluorescence anisotropy in particular, is a useful and favourable tool to study biochemical problems.

Original languageEnglish
Pages (from-to)225-229
Number of pages5
JournalDyes and Pigments
Issue number2
Publication statusPublished - Nov 2009


  • Bioconjugation
  • Fluorescein-5-maleimide
  • Fluorescence anisotropy
  • Glutathione S-transferase (GST)
  • Protein-antibody interaction

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Process Chemistry and Technology


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