期刊
ANALYTICA CHIMICA ACTA
卷 625, 期 1, 页码 103-109出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.aca.2008.07.021
关键词
fluorescence correlation spectroscopy; association and dissociation kinetics; protein interaction
In this article, we present a systematic study on IgG and Fab fragment of anti-IgG molecules using fluorescence auto- and cross-correlation spectroscopy to investigate their diffusion characteristics, binding kinetics, and the effect of small organic molecule, urea on their binding. Through our analysis, we found that the diffusion coefficient for IgG and Fab fragment of anti-IgG molecules were 37 +/- 2 mu m(2) s(-1) and 56 +/- 2 mu m(2) s(-1), respectively. From the binding kinetics study, the respective forward (k(a)) and backward (k(d)) reaction rates were (5.25 +/- 0.25) x 10(6) M-1 s(-1) and 0.08 +/- 0.005 s(-1), respectively and the corresponding dissociation binding constant (K-D) was 15 +/- 2 nM. We also found that urea inhibits the binding of these molecules at 4 M concentration due to denaturation. (c) 2008 Elsevier B.V. All rights reserved.
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