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

Electrophoretic Investigations of the Acid Conformational Change of α-Lactalbumin

https://ir.soken.ac.jp/records/4111
https://ir.soken.ac.jp/records/4111
741c6da1-d09e-4e4e-bca9-f429b6990d73
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 Electrophoretic Investigations of the Acid Conformational Change of α-Lactalbumin
タイトル
タイトル Electrophoretic Investigations of the Acid Conformational Change 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 KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

Search repository
NITTA, Katsutoshi

× NITTA, Katsutoshi

NITTA, Katsutoshi

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 In order to clarify how the electrophoretic behavior reflects the conformational transition of globular proteins, moving boundary electrophoresis was applied to analysis of the acid conformational change of α-lactalbumin. The appearance of only a single electrophoretic boundary in the transition region of the protein suggests a very rapid transition with a half-time estimated to be smaller than 7 min on the basis of the theory of isomerizing systems in electrophoresis. The transition is clearly reflected in the dependence of the mobility on the protein net charge, which shows a sigmoidal curve closely similar to that obtained by a LinderstrømLang pH-titration plot for the carboxyl groups of α-lactalbumin. It was also concluded from the transition curves that the acidfication does not result in complete unfolding, but that a compact structure is maintained in the acidic region with an apparently expanded form as compared to the native state of the protein. All results obtained by electrophoresis were also supported by the results of pH-jump studies, analytical gel chromatography, and CD measurements.
書誌情報 Journal of Biochemistry
en : Journal of Biochemistry

巻 78, 号 1, p. 205-211, 発行日 1975
出版者
出版者 Oxford University Press
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021924X
PubMed番号
識別子タイプ PMID
関連識別子 376
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1093/oxfordjournals.jbchem.a130885
関連名称 10.1093/oxfordjournals.jbchem.a130885
権利
権利情報 © The Japanese Biochemical Society
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:27:39.140156
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