Protein Bindings. VI. Binding of Phenols to Bovine Serum Albumin
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概要
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Binding constant, K, for 23 phenols with bovine serum albumin was evaluated spectrophotometrically utilizing the albumin-induced metachromasia of 2-(4'-hydroxyphenylazo)-benzoic acid. In the binding, electrostatic force seems dominant but hydrophobic binding may not be negligible with 2,4-dichlorophenol and 2,4,5-trichlorophenol. The values of log K generally correlated with pK_a, in vitro bacteriostatic activity against Staphylococcus aureus 209 P, action of uncoupling oxidative phosphorylation at mitochondria, and π-electron-density for the oxygen-atom of phenolic hydroxy group of phenols,
- 公益社団法人日本薬学会の論文
- 1969-02-25
著者
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森口 郁生
School of Pharmaceutical Sciences, Kitasato University
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森口 郁生
School Of Pharmaceutical Sciences Kitasato University
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富岡 穂一
Research Laboratory, Chugai Pharmaceutical Co., Ltd.
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和田 栄
Research Laboratories, Chugai Pharmaceutical Co., Ltd.
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和田 栄
Research Laboratories Chugai Pharmaceutical Co. Ltd.
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富岡 穂一
Research Laboratory Chugai Pharmaceutical Co. Ltd.
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