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Influence of Ca2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra
https://ir.soken.ac.jp/records/4132
https://ir.soken.ac.jp/records/4132a4e16cd4-3ecd-4705-ade2-68bda466519f
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-01-08 | |||||
| タイトル | ||||||
| タイトル | Influence of Ca2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra | |||||
| タイトル | ||||||
| タイトル | Influence of Ca2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra | |||||
| 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× HARUSHIMA, Yoshiaki× SUGAI, Shintaro |
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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 | Both the Ca2+-bound and Ca2+-free forms of α-lactalbumin can assume essentially the same folded conformation as evidenced by similarity in their CD and proton n.m.r. spectra. Thermal unfolding followed by the aromatic CD has shown that the stability of the folded state is markedly enhanced by Ca2+ and that the stabilization is almost entirely entropic; addition of 0.1 mM Ca2+ shifts the transition temperature from 40° to 62° in 0.1 M Na+ at pH 7.0. The enthalpy change of the unfolding, coincident between the two forms, is, however, significantly smaller than that known for lysozyme. The n.m.r. spectrum under the condition that both the forms of the protein are in the folded state reflects minor environmental changes of certain protons upon Ca2+ binding, and these changes are shown to afford useful probes for assessment of the location of the binding site. From the pH dependence and temperature dependence of the spectrum and also by using spin decoupling in the aromatic region (6.4–8.7 p.p.m.), it is shown that none of histidyl residues are affected and that at least two tryptophanyl ring protons experience environmental changes upon Ca2+ binding to the folded apo-protein. Effect of free excess Ca2+ on the spectrum has also shown that in native α-lactalbumin there is only one Ca2+-binding site that is detectable by the present method. | |||||
| 書誌情報 |
International Journal of Peptide and Protein Research en : International Journal of Peptide and Protein Research 巻 27, 号 1, p. 18-27, 発行日 1986-01 |
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| 出版者 | ||||||
| 出版者 | Wiley-Blackwell | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 03678377 | |||||
| PubMed番号 | ||||||
| 識別子タイプ | PMID | |||||
| 関連識別子 | 3949437 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1111/j.1399-3011.1986.tb02761.x | |||||
| 関連名称 | 10.1111/j.1399-3011.1986.tb02761.x | |||||
| 権利 | ||||||
| 権利情報 | © 1986 Munksgaard International Publishers Ltd. | |||||
