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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

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/4290
474a498e-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
言語 en
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
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

WEKO 1929

FUJIKAWA, Kazuo

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ARAI, Munehito

× ARAI, Munehito

WEKO 2491

ARAI, Munehito

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SHIMIZU, Akio

× SHIMIZU, Akio

WEKO 2505

SHIMIZU, Akio

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IKEGUCHI, Masamichi

× IKEGUCHI, Masamichi

WEKO 2379

IKEGUCHI, Masamichi

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

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SUGAI, Shintaro

× SUGAI, Shintaro

WEKO 2363

SUGAI, Shintaro

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著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
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
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
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