Interaction of Ada protein with DNA examined by fluorescence anisotropy of the protein.
作者： Masayuki Takahashi , Kunihiko Sakumi , Mutsuo Sekiguchi
DOI: 10.1021/BI00466A002
关键词: DNA 、 Biophysics 、 Plasma protein binding 、 Base pair 、 A-DNA 、 O-6-methylguanine-DNA methyltransferase 、 Binding site 、 Fluorescence anisotropy 、 Analytical chemistry 、 Chemistry 、 Fluorescence spectrometry
摘要: We made use of enhancement fluorescence anisotropy protein upon DNA binding to analyze interactions between Ada and DNA. is a repair enzyme that also acts as transcription regulator. The isotropic was not significantly affected interaction with could be used signal for detection the binding. did became larger because reduces diffusion protein. change reproducible independent concentration degree saturation when large; these values can readily converted proportion complexed parameters were then determined by direct comparison experimental theoretical variations anisotropy, increasing concentrations computed considering overlap potential sites on lattice [McGhee & von Hippel (1974) J. Mol. Biol. 86, 469-489]. Binding does seem occur in cooperative manner. number base pairs covered monomer 7 +/- 1; this salt concentration. equilibrium association constant decreased from 4 X 10(7) 3 10(5) M-1 an increase NaCl 0.1 0.2 M, thereby indicating possible involvement ionic phosphate groups
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