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Fluorescence anisotropy analysis of protein–antibody interaction
Authors:Nadia Barbero  Lucia Napione  Pierluigi Quagliotto  Simona Pavan  Claudia Barolo  Ermanno Barni  Federico Bussolino  Guido Viscardi
Affiliation:1. Institute of Material Science, Vietnam Academy of Science and Technology, 18, Hoang Quoc Viet Road, Cau Giay, Hanoi, Viet Nam;2. Research Center for Environmental Technology and Sustainable Development, Hanoi University of Science, Hanoi, Viet Nam;3. School of Chemical Engineering, Hanoi University of Science and Technology, 1, Dai Co Viet Road, Hanoi, Viet Nam;4. Department of Chemistry, Hanyang University, Seoul 133-791, Republic of Korea
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.
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