Fluorescence anisotropy analysis of protein–antibody interaction

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 bindi...

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Bibliographic Details
Published in:Dyes and pigments 2009-11, Vol.83 (2), p.225-229
Main Authors: Barbero, Nadia, Napione, Lucia, Quagliotto, Pierluigi, Pavan, Simona, Barolo, Claudia, Barni, Ermanno, Bussolino, Federico, Viscardi, Guido
Format: Article
Language:English
Subjects:
Bioconjugation
Fluorescein-5-maleimide
Fluorescence anisotropy
Glutathione S-transferase (GST)
Protein–antibody interaction
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Summary: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, K d and K a; 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.
ISSN:0143-7208
1873-3743
DOI:10.1016/j.dyepig.2009.04.011