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Three-State denaturation of α-lactalbumin by guanidine-hydrochloride
https://ir.soken.ac.jp/records/4112
https://ir.soken.ac.jp/records/4112b964c9ee-89a7-444b-af6f-f5fc6356198a
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||||
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| 公開日 | 2013-12-24 | |||||||||||||
| タイトル | ||||||||||||||
| タイトル | Three-State denaturation of α-lactalbumin by guanidine-hydrochloride | |||||||||||||
| タイトル | ||||||||||||||
| タイトル | Three-State denaturation of α-lactalbumin by guanidine-hydrochloride | |||||||||||||
| 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 | |||||||||||||
| アクセス権 | ||||||||||||||
| アクセス権 | metadata only access | |||||||||||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||||||||||
| 著者 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro
× NITTA, Katsutoshi
× YONEYAMA, Michio
× SUGAI, Shintaro
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| 著者別名 |
桑島, 邦博
× 桑島, 邦博
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| 抄録 | ||||||||||||||
| 内容記述タイプ | Abstract | |||||||||||||
| 内容記述 | The reversible unfolding of α-lactalbumin by guanidine hydrochloride has been studied at 25.0 °C by means of ultraviolet circular dichroism measurements. The non-coincidence of the apparent transition curves obtained from the ellipticity changes at far (222 nm) and at near (270 nm and 296 nm) ultraviolet wave-lengths demonstrates the presence of at least one intermediate in the denaturation process. The aromatic residues which contribute to the Cotton effects at 270 nm and at 296 nm appear to be exposed to solvent in the first stage of a two-stage process, while the helical regions of the polypeptide chain appear to be destroyed in the second stage. Earlier work has demonstrated an acid transition between two compact forms of α-lactalbumin, a native (neutral pH) form and an acid form. Results presented here suggest that the acid form is produced as an intermediate in the first stage of total unfolding at neutral pH. Lysozyme and α-lactalbumin are known to have similar primary structures and are expected to have similar tertiary structures, but several differences in their properties have been described. The comparison of the unfolding transitions of α-lactalbumin and lysozyme provides a result compatible with similar tertiary structures, although the free energy of stabilization of the native state is 3 to 5 kcal/mol smaller for α-lactalbumin than for lysozyme. The pH dependence of the unfolding reaction can be described in terms of abnormal histidyl and carboxyl residues. The presence of a stable intermediate in the denaturation process may cause a difference in dynamic character in the native state between the two proteins and thus provide a reasonable interpretation for their known differences in chemical reactivity. |
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| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 106, 号 2, p. 359-378, 発行日 1976-09-15 |
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| 出版者 | ||||||||||||||
| 出版者 | Elsevier | |||||||||||||
| ISSN | ||||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||||
| 収録物識別子 | 0022-2836 | |||||||||||||
| PubMed番号 | ||||||||||||||
| 識別子タイプ | PMID | |||||||||||||
| 関連識別子 | 10445 | |||||||||||||
| DOI | ||||||||||||||
| 識別子タイプ | DOI | |||||||||||||
| 関連識別子 | https://doi.org/10.1016/0022-2836(76)90091-7 | |||||||||||||
| 関連名称 | 10.1016/0022-2836(76)90091-7 | |||||||||||||
| 権利 | ||||||||||||||
| 権利情報 | © 1976 Published by Elsevier Ltd | |||||||||||||
