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

Three-State denaturation of α-lactalbumin by guanidine-hydrochloride

https://ir.soken.ac.jp/records/4112
https://ir.soken.ac.jp/records/4112
b964c9ee-89a7-444b-af6f-f5fc6356198a
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-12-24
タイトル
タイトル Three-State denaturation of α-lactalbumin by guanidine-hydrochloride
タイトル
タイトル Three-State denaturation of α-lactalbumin by guanidine-hydrochloride
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 KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

Search repository
NITTA, Katsutoshi

× NITTA, Katsutoshi

NITTA, Katsutoshi

Search repository
YONEYAMA, Michio

× YONEYAMA, Michio

YONEYAMA, Michio

Search repository
SUGAI, Shintaro

× SUGAI, Shintaro

SUGAI, Shintaro

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 reversible unfolding of α-lactalbumin by guanidine hydrochloride has been studied at 25.0 °C by means of ultraviolet circular dichroism measurements. The non-coincidence of the apparent transition curves obtained from the ellipticity changes at far (222 nm) and at near (270 nm and 296 nm) ultraviolet wave-lengths demonstrates the presence of at least one intermediate in the denaturation process. The aromatic residues which contribute to the Cotton effects at 270 nm and at 296 nm appear to be exposed to solvent in the first stage of a two-stage process, while the helical regions of the polypeptide chain appear to be destroyed in the second stage. Earlier work has demonstrated an acid transition between two compact forms of α-lactalbumin, a native (neutral pH) form and an acid form. Results presented here suggest that the acid form is produced as an intermediate in the first stage of total unfolding at neutral pH.

Lysozyme and α-lactalbumin are known to have similar primary structures and are expected to have similar tertiary structures, but several differences in their properties have been described. The comparison of the unfolding transitions of α-lactalbumin and lysozyme provides a result compatible with similar tertiary structures, although the free energy of stabilization of the native state is 3 to 5 kcal/mol smaller for α-lactalbumin than for lysozyme. The pH dependence of the unfolding reaction can be described in terms of abnormal histidyl and carboxyl residues. The presence of a stable intermediate in the denaturation process may cause a difference in dynamic character in the native state between the two proteins and thus provide a reasonable interpretation for their known differences in chemical reactivity.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 106, 号 2, p. 359-378, 発行日 1976-09-15
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
PubMed番号
識別子タイプ PMID
関連識別子 10445
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/0022-2836(76)90091-7
関連名称 10.1016/0022-2836(76)90091-7
権利
権利情報 © 1976 Published by Elsevier Ltd
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:27:38.471734
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