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Folding−Unfolding Equilibrium and Kinetics of Equine β-Lactoglobulin: Equivalence between the Equilibrium Molten Globule State and a Burst-Phase Folding Intermediate
https://ir.soken.ac.jp/records/4290
https://ir.soken.ac.jp/records/4290474a498e-bca9-4793-aa00-20a1a61f4291
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-13 | |||||
| タイトル | ||||||
| タイトル | Folding−Unfolding Equilibrium and Kinetics of Equine β-Lactoglobulin: Equivalence between the Equilibrium Molten Globule State and a Burst-Phase Folding Intermediate | |||||
| タイトル | ||||||
| タイトル | Folding−Unfolding Equilibrium and Kinetics of Equine β-Lactoglobulin: Equivalence between the Equilibrium Molten Globule State and a Burst-Phase Folding Intermediate | |||||
| 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 |
FUJIKAWA, Kazuo
× FUJIKAWA, Kazuo× ARAI, Munehito× SHIMIZU, Akio× IKEGUCHI, Masamichi× KUWAJIMA, Kunihiro× 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 denaturant-induced equilibrium unfolding transition of equine β-lactoglobulin was investigated by ultraviolet absorption, fluorescence, and circular dichroism (CD) spectra. An equilibrium intermediate populates at moderate denaturant concentrations, and its CD spectrum is similar to that of the molten globule state previously observed for this protein at acid pH [Ikeguchi, M., Kato, S., Shimizu, A., and Sugai, S. (1997) Proteins: Struct., Funct., Genet. 27, 567−575]. The unfolding and refolding kinetics were also investigated by the stopped-flow CD and fluorescence. A significant change in the CD intensity was observed within the dead time of measurements (25 ms) when the refolding reaction was initiated by diluting the urea-unfolded protein solution, indicating the transient accumulation of the folding intermediate. The CD spectrum of this burst-phase intermediate agrees well with that of the molten globule state at acid pH. The stability of the burst-phase intermediate was also estimated from the urea-concentration dependence of the burst-phase amplitude, and it shows a fair agreement with that of the equilibrium intermediate. These results indicate that the molten globule state of equine β-lactoglobulin populates at moderate urea concentration as well as at acid pH and it is equivalent with the kinetic folding intermediate. | |||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 38, 号 14, p. 4455-4463, 発行日 1999 |
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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 | 0006-2960 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | http://doi.org/10.1021/bi982683p | |||||
| 関連名称 | 10.1021/bi982683p | |||||
| 権利 | ||||||
| 権利情報 | © 1999 American Chemical Society | |||||
