Archivio Istituzionale della RicercaThe 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. © 2009 Elsevier Ltd. All rights reserved.
Fluorescence anisotropy analysis of protein-antibody interaction / Barbero, N.; Napione, L.; Quagliotto, P.; Pavan, S.; Barolo, C.; Barni, E.; Bussolino, F.; Viscardi, G.. - In: DYES AND PIGMENTS. - ISSN 0143-7208. - 83:2(2009), pp. 225-229. [10.1016/j.dyepig.2009.04.011]
Fluorescence anisotropy analysis of protein-antibody interaction
Napione L.;
2009
Abstract
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. © 2009 Elsevier Ltd. All rights reserved.
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https://hdl.handle.net/11583/3009313