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Circular Dichroism Quantitative Estimate of α-Helix Content of Human Serum Albumin in the Presence of NaSCN, Urea and KCl at Various pH
https://kwmed.repo.nii.ac.jp/records/148
https://kwmed.repo.nii.ac.jp/records/148f6064f17-0446-46b0-a679-391ca83f01a0
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00010223719.pdf (11.2 MB)
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| Item type | [ELS]学術雑誌論文 / Journal Article(1) | |||||||||
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| 公開日 | 2017-01-23 | |||||||||
| タイトル | ||||||||||
| タイトル | Circular Dichroism Quantitative Estimate of α-Helix Content of Human Serum Albumin in the Presence of NaSCN, Urea and KCl at Various pH | |||||||||
| 言語 | en | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||
| 資源タイプ | journal article | |||||||||
| 著者 |
WATANABE, Satoru
× WATANABE, Satoru
× SAITO, Taiichi
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| 著者所属(英) | ||||||||||
| en | ||||||||||
| Department of Pharmacology, Kawasaki Medical School | ||||||||||
| 著者所属(英) | ||||||||||
| en | ||||||||||
| Department of Pharmacology, Kawasaki Medical School | ||||||||||
| キーワード | ||||||||||
| 言語 | en | |||||||||
| 主題Scheme | Other | |||||||||
| 主題 | Circular dichroism | |||||||||
| キーワード | ||||||||||
| 言語 | en | |||||||||
| 主題Scheme | Other | |||||||||
| 主題 | Human serum albumin | |||||||||
| キーワード | ||||||||||
| 言語 | en | |||||||||
| 主題Scheme | Other | |||||||||
| 主題 | Conformational alteration | |||||||||
| キーワード | ||||||||||
| 言語 | en | |||||||||
| 主題Scheme | Other | |||||||||
| 主題 | Sodium thiocyanate | |||||||||
| 記事種別(英) | ||||||||||
| 内容記述タイプ | Other | |||||||||
| 内容記述 | Original Article | |||||||||
| 言語 | en | |||||||||
| 抄録(英) | ||||||||||
| en | ||||||||||
| Conformational changes in human serum albumin (HSA) in the presence of several concentrations of NaSCN, urea and KCl at various pH were examined quantitatively on the basis of rotational strength at 208 nm by means of circular dichroism (CD). The α-helix content of HSA was markedly dependent on concentrations of NaSCN and urea, but not on KCl. However, when these salts coexisted with a concentration of hydrogen ion in the albumin solution, the α-helix content of HSA was markedly dependent on all these salts. Among these salts, the distortion power of NaSCN on the conformational stability of the peptide backbone was undoubtedly several hundred times stronger than that of the other salts. Conformational changes in HSA were scarcely observed at pH 4.8-10.0 under a constant concentration of each salt, but were more dependent on pH outside of the above range regardless of salt. The α-helix content of highly denaturated HSA in solution containing a high salt concentration was less dependent on the hydrogen ion concentration, while at a low concentration of each salt, it was pH dependent, as if there was no salt. | ||||||||||
| 書誌情報 |
en : Kawasaki medical journal 巻 11, 号 2, p. 93-100, 発行日 1985 |
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| URL | ||||||||||
| 識別子 | http://igakkai.kms-igakkai.com/wp/wp-content/uploads/1985en/11(2)93-100.1985.pdf | |||||||||
| 識別子タイプ | URI | |||||||||
| DOI | ||||||||||
| 識別子タイプ | DOI | |||||||||
| 関連識別子 | https://doi.org/10.11482/KMJ-E11(2)93 | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | PISSN | |||||||||
| 収録物識別子 | 0385-0234 | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | EISSN | |||||||||
| 収録物識別子 | 2434-3404 | |||||||||
| 雑誌書誌ID | ||||||||||
| 収録物識別子タイプ | NCID | |||||||||
| 収録物識別子 | AA00710169 | |||||||||
| 雑誌書誌ID | ||||||||||
| 収録物識別子タイプ | NCID | |||||||||
| 収録物識別子 | AA12029005 | |||||||||
| 著者版フラグ | ||||||||||
| 出版タイプ | VoR | |||||||||
