Multiple classes of binding sites for palmitic acid on the fatty acid-binding protein molecule |
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Authors: | F Fukai T Kase T Shidotani T Nagai T Katayama |
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Institution: | Department of Patho-Physiology, Faculty of Pharmaceutical Sciences, Science University of Tokyo. |
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Abstract: | Binding characteristics of fatty acid-binding protein (FABP) toward palmitic acid were studied. On the analysis of the interaction between FABP and 3H]palmitic acid over a wide range of concentrations of the fatty acid, at least three saturation plateaux were observed. By Scatchard-plot analysis, it appeared that FABP possesses three classes of binding sites for palmitic acid with different affinities Kd1 = 1 x 10(-6) M (N = 1), Kd2 = 4 x 10(-6) M (N = 2), Kd3 = 2 x 10(-5) M (N = 10)]. Results of both sedimentation analyses and chromatofocusing of FABPs labeled with various concentrations of 3H]palmitic acid suggested that the FABP used was homogeneous. These results indicate that several classes of binding sites for palmitic acid with different affinities are present on the FABP molecule. |
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