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Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin
https://ir.soken.ac.jp/records/4273
https://ir.soken.ac.jp/records/42735f2fee6b-f172-4189-aedd-fcd2ca82527f
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2014-03-10 | |||||
タイトル | ||||||
タイトル | Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin | |||||
タイトル | ||||||
タイトル | Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin | |||||
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 |
KATSUMATA, Kumiko
× KATSUMATA, Kumiko× OKAZAKI, Akira× 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 effect of GroEL on the re-folding kinetics of apo- and holo-α-lactalbumin from the acidic molten globule state has been investigated by stopped-flow fluorescence measurements. GroEL retards the re-folding of apo-α-lactalbumin by interacting with the molten globule state of the protein. The binding constant was estimated to be in the order of 105M−1by analyzing the kinetic data quantitatively and was found to be much weaker than the binding between GroEL and disulfide-bond reduced α-lactalbumin, whose binding constant is in the order of 107M−1. Our present results, together with the previous results, suggest that the state recognized by GroEL is not unique and that the binding strength varies with the state of a target protein. The binding between GroEL and the molten globule state of apo-α-lactalbumin becomes stronger with an increasing salt concentration; the binding constant is increased tenfold (from 105to 106M−1) by an increase in salt concentration from 0.05 to 0.25 M. The study of the effect of GroEL on the re-folding kinetics of holo-α-lactalbumin, which is represented by a bi-phasic process, shows that the slow phase is affected by GroEL in the same manner as observed in the apo-α-lactalbumin re-folding but that the fast phase is not affected by GroEL at all. This indicates that the binding rate of GroEL is faster than the slow phase but slower than the fast phase of the re-folding, and the bi-molecular rate constant of GroEL binding to the molten globule state of α-lactalbumin was estimated to be in the order of 106M−1s−1. | |||||
書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 258, 号 5, p. 827-838, 発行日 1996-05-24 |
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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 | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1006/jmbi.1996.0290 | |||||
関連名称 | 10.1006/jmbi.1996.0290 | |||||
権利 | ||||||
権利情報 | © 1996 Academic Press |