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

Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin

https://ir.soken.ac.jp/records/4273
https://ir.soken.ac.jp/records/4273
5f2fee6b-f172-4189-aedd-fcd2ca82527f
Item type 学術雑誌論文 / Journal Article(1)
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

KATSUMATA, Kumiko

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OKAZAKI, Akira

× OKAZAKI, Akira

OKAZAKI, Akira

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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著者別名 桑島, 邦博

× 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
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
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