Study of Protein Adsorption on Glass Surfaces with a Hydrophobic Fluorescent Probe
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概要
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The relationship between the affinity of proteins for glass surfaces in a water medium and the fluorescence intensity of a probe [7-(p-methoxybenzylamino)-4-nitrobenz-2-oxa-1,3-diazole (MBD)] of hydrophobic areas on proteins was studied. Proteins displaying a weak affinity for glass surfaces, such as bovine serum albumin and horse-radish peroxidase, showed stronger fluorescence than those displaying a stronger affinity for glass surfaces, such as serum globulin and fibrinogen. Compatible results were obtained in the chromatography of protein mixtures, such as serum or extract of liver, on porous glass columns. These results suggest that hydrophobic interactions do not participate in the adsorption of proteins on glass surfaces.
- 公益社団法人日本薬学会の論文
- 1984-06-25
著者
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水谷 隆治
Faculty Of Pharmaceutical Sciences Nagoya City University
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浅岡 文子
Faculty of Pharmaceutical Sciences, Nagoya City University
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浅岡 文子
Faculty Of Pharmaceutical Sciences Nagoya City University
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水谷 隆治
Faculty of Pharmaceutical Sciences
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