Thyroxine Binding Properties of Glycosylated Human Serum Albumin as Measured by Fluorescence
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概要
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Thyroid hormone, thyroxine (T_4) binding to glycosylated human serum albumin (G-HSA), and native human serum albumin (HSA) were studied as a function of pH using the fluorescence method. T_4 binding affinity for G-HSA was remarkably reduced in an alkaline pH as compared with the native HSA. The thermodynamic parameters for binding are estimated at pH 7.5 : (a) for G-HSA, ΔG=-8.50±0.04 kcal mol^<-1> (30℃), ΔH=-5.2 kcal mol^<-1>, ΔS=+11 e. u. ; (b) for HSA, ΔG=-8.89±0.04 kcal mol^<-1> (30℃), ΔH=-3.5 kcal mol^<-1>, ΔS=+18 e. u. These results suggest that the glycosylation of HSA causes a variation in the electrostatic interaction between T_4 and HSA.
- 公益社団法人日本薬学会の論文
- 1995-01-15
著者
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岡部 亘雄
Faculty of Pharmaceutical Sciences, Kinki University
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岡部 亘雄
Faculty Of Pharmaceutical Sciences Kinki University
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吉田 彩斗子
Faculty Of Pharmaceutical Sciences Kinki University
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