Some characteristics of cytosol binding protein for 1.ALPHA.,25-dihydroxycholecalciferol and 25-hydroxycholecalciferol in rat intestinal mucosa.
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概要
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Cytosol binding protein for 1α, 25-(OH)2D3 and 25-OHD3 was demonstrated in rat intestinal mucosa using sucrose density gradient ultracentrifugation analysis, Sephadex G-200 column chromatography and polyacrylamide disc gel electrophoresis. The binding protein has a sedimentation constant of 5-6S, a molecular weight of 100, 000-120, 000 daltons and a mobility in electrophoresis of Rf 0.42. Further analysis of binding behavior by DEAE-cellulose filter assays revealed that the binding protein had a higher affinity for 25-OHD3 than for 1α, 25-(OH)2D3, and that 1α, 25-(OH)2D3 competed with 25-OHD3 for the same binding site on the protein. The apparent dissociation constant for 1α, 25-(OH)2D3 and 25-OHD3 was 9.2×10-9 M and 1.5×10-9 M, respectively. The binding capacity was 3.1 pmoles/mg protein for both 1α, 25-(OH)2D3 and 25-OHD3. The order of binding affinity was 25-OHD3>1α, 25-(OH)2D3>>D3=1α-OHD3
- 財団法人 学会誌刊行センターの論文
著者
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志村 二三夫
Department of Nutrition, School of Health Sciences, Faculty of Medicine, University of Tokyo
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森内 幸子
Department of Food and Nutrition, Faculty of Home Economics, Japan Women's University
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細谷 憲政
Department fo Nutrition, School of Health Sciences, Faculty of Medicine, University of Tokyo
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