ログイン
言語:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

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

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/4150
14a57adf-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

IKEGUCHI, Masamichi

Search repository
SUGAI, Shintaro

× SUGAI, Shintaro

SUGAI, Shintaro

Search repository
FUJINO, Motoaki

× FUJINO, Motoaki

FUJINO, Motoaki

Search repository
SUGAWARA, Tatsuro

× SUGAWARA, Tatsuro

SUGAWARA, Tatsuro

Search repository
KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

桑島, 邦博

Search repository
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
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
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:27:15.930356
Show All versions

Share

Mendeley Twitter Facebook Print Addthis

Cite as

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR 2.0
  • OAI-PMH JPCOAR 1.0
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX

Confirm


Powered by WEKO3


Powered by WEKO3