Adsorption of bovine serum albumin on the surface of ultrafine silica modified by trimethylsilyl groups
The adsorption of bovine serum albumin (BSA) on the surface of hydroрhilic and partially hydroрhobic ultrafine silica modified by hexamethyldisilasan was investigated. The adsorption was carried out from aqueous and aqueous-salt solutions at рН 4,8 and 7,4 and obtained adsorption isotherms were char...
Збережено в:
| Дата: | 2009 |
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| Автори: | , , , |
| Формат: | Стаття |
| Мова: | Російська |
| Опубліковано: |
Chuiko Institute of Surface Chemistry National Academy of Sciences of Ukraine
2009
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| Онлайн доступ: | https://surfacezbir.com.ua/index.php/surface/article/view/333 |
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| Назва журналу: | Surface |
| Завантажити файл: |  |
Репозитарії
Surface| Резюме: | The adsorption of bovine serum albumin (BSA) on the surface of hydroрhilic and partially hydroрhobic ultrafine silica modified by hexamethyldisilasan was investigated. The adsorption was carried out from aqueous and aqueous-salt solutions at рН 4,8 and 7,4 and obtained adsorption isotherms were characterized. IR-spectra of adsorbed protein on silica were obtained and discussed. It was shown that the hydrogen bonds between isolated hydroxyl groups of silica and NH-groups of protein were formed as a result of protein adsorption. The changes of the secondary structure of the protein adsorbed on partially hydroрhobic silica are discussed. |
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