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Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of its native and molten globule states
https://ir.soken.ac.jp/records/4150
https://ir.soken.ac.jp/records/415014a57adf-d046-4cec-bfb8-ba2cd96d139a
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-01-17 | |||||
| タイトル | ||||||
| タイトル | Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of its native and molten globule states | |||||
| タイトル | ||||||
| タイトル | Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of its native and molten globule states | |||||
| 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 |
IKEGUCHI, Masamichi
× IKEGUCHI, Masamichi× SUGAI, Shintaro× FUJINO, Motoaki× SUGAWARA, Tatsuro× KUWAJIMA, Kunihiro |
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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 unfolding and refolding of a derivative of a-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selectively reduced and S-carboxymethylated, are investigated by equilibrium and kinetic circular dichroism measurements. The native conformation of this derivative is known to be essentially identical to that of intact α-lactalbumin. The equilibrium unfolding of the derivative involves a stable intermediate, which is also similar to the molten globule state of the disulfide intact protein. The results of stopped-flow circular dichroism experiments show that the same intermediate is formed rapidly as a transient intermediate in kinetic refolding. The conformational stabilities for the native and intermediate states have been estimated and compared with the stabilities for the corresponding states of intact α-lactalbumin. The stabilization of the native state by the disulfide has been interpreted in terms of a decrease in chain entropy in the unfolded state and elimination of the strain imposed on the disulfide bond in the native state. The molten globule state is also stabilized by the disulfide bond, although the degree of stabilization of the molten globule state is smaller than of the native state. The results suggest that, in the molten globule state, some ordered structures are present within the loop moiety formed by the 6-120 disulfide. | |||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 31, 号 50, p. 12695-12700, 発行日 1992 |
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| 出版者 | ||||||
| 出版者 | American Chemical Society | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 00062960 | |||||
| PubMed番号 | ||||||
| 識別子タイプ | PMID | |||||
| 関連識別子 | 1472507 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | http://doi.org/10.1021/bi00165a021 | |||||
| 関連名称 | 10.1021/bi00165a021 | |||||
| 権利 | ||||||
| 権利情報 | © 1992 American Chemical Society | |||||
