Fluorescence anisotropy analysis of protein-antibody interaction

The interaction between glutathione S-transferase and its antibody alpha-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. (C) 2009 Elsevier Ltd. All rights reserved.