Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
177364 | Dyes and Pigments | 2009 | 5 Pages |
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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Nadia Barbero, Lucia Napione, Pierluigi Quagliotto, Simona Pavan, Claudia Barolo, Ermanno Barni, Federico Bussolino, Guido Viscardi,