Effect of pH Small Inorganic Ions on Binding of Sulfadimethoxine and Sulfaphenazole to Human Serum Albumin Measured by Circular Dichroism
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概要
- 論文の詳細を見る
The binding of sulfadimethoxine and sulfaphenazole to human serum albumin (HSA) has been shown by circular dichroism measurements to be dependent on the N-B transition. The secondary drug binding sites were found to be optically active in the B conformation form in HSA but optically inactive in the N form. Moreover, the drug-HSA interaction in Tris-HCl buffer seems to be more sensitive to the conformational change in HSA, compared with that in the phosphate buffer.
- 社団法人日本薬学会の論文
- 1989-05-25
著者
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小田切 優樹
Faculty of Pharmaceutical Science, Kumamoto University
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中村 英樹
Faculty of Pharmaceutical Sciences, Kumamoto University
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今村 順茂
Faculty of Pharmaceutical Sciences, Kumamoto University
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今村 順茂
熊本大学薬学部
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中村 英樹
Faculty Of Pharmaceutical Sciences Kumamoto University
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今村 順茂
Faculty Of Pharmaceutical Sciences Kumamoto University
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松本 潮
Tokyo College of Pharmacy
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FLEITMAN Jeff
College of Pharmacy, University of Florida
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PERRIN H.
College of Pharmacy, University of Florida
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Fleitman Jeff
College Of Pharmacy University Of Florida
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Perrin H.
College Of Pharmacy University Of Florida
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