A Thermodynamic Study of Albumin Adsorption onto Some Solid Surfaces
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概要
- 論文の詳細を見る
In order to understand protein adsorption, the thermodynamic parameters were evaluated from the initial slope of the isotherms of human albumin adsorption onto glass, Biomer (a hydrophobic plyurethane), 2-600 (a hydrophilic polyurethane) and silicone surfaces. The Gibbs free energy (ΔG) values of albumin adsorption in 10 mM phosphate buffer at pH 7.35 and at 23℃ were -5.24,-6.46,-4.55 and -7.21kcal/mol, respectively. These values changed in 1M NaCl-10mM phosphate to -3.75,-6.99,-4.57 and -8.21kcal/mol, respectively. There was a clear influence of salt concentration on the ΔG values of albumin adsorption on glass surfaces in the range of 0-0.5M NaCl in the phosphate buffer.
- 公益社団法人日本薬学会の論文
- 1988-07-25
著者
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水谷 隆治
Faculty of Pharmaceutical Sciences, Nagoya City University
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水谷 隆治
Faculty Of Pharmaceutical Sciences Nagoya City University
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BRASH JOHN
Department of Chemical Engineering and pathology, Mc Master University
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Brash John
Department Of Chemical Engineering And Pathology Mc Master University
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水谷 隆治
Faculty of Pharmaceutical Sciences
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