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Ca2+-induced alteration in the unfolding behavior of α-lactalbumin
https://ir.soken.ac.jp/records/4133
https://ir.soken.ac.jp/records/413367d10e35-6346-4d18-aba2-7aa2f304a0cc
| 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 | Ca2+-induced alteration in the unfolding behavior of α-lactalbumin | |||||
| タイトル | ||||||
| タイトル | Ca2+-induced alteration in the unfolding behavior 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 |
IKEGUCHI, Masamichi
× IKEGUCHI, Masamichi× KUWAJIMA, Kunihiro× 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 | Comparative studies of the unfolding equilibria of two homologous proteins, bovine α-lactalbumin and hen lysozyme, induced by treatment with guanidine hydrochloride have been made by analysis of the peptide and the aromatic circular dichroism spectra. The effect of the specific binding of Ca2+ ion by the former protein was taken into account in interpreting the unfolding equilibria of the protein. Proton nuclear magnetic resonance spectra of α-lactalbumin were also measured for the. purpose of characterizing an intermediate structural state of the protein. In previous studies, α--lactalbumin was shown to be an exceptional protein whose equilibrium unfolding does not obey the two-state model of unfolding, although lysozyme is known to follow the two-state unfolding mechanism. The present results show that the apparent unfolding behavior of α-lactalbumin depends on Ca2+ concentration. At a low concentration of Ca2+, α-lactalbumin unfolds with a stable intermediate that has unfolded tertiary structure, as evidenced by the featureless nuclear magnetic resonance and aromatic circular dichroism spectra, but has folded secondary structure as evidenced by the peptide circular dichroism spectra. However, in the presence of a sufficiently high concentration of Ca2+ the unfolding transition of α-lactalbumin resembles that of lysozyme. The transition occurs between the two states, the native and the fully unfolded states, and the cooperativity of the unfolding is essentially the same as that of lysozyme. Such a change in the apparent unfolding behavior evidently results from an increase in the stability of the native state relative to that of the intermediate induced by the specific Ca2+ binding to native α-lactalbumin. The results are useful for understanding the relationship between the protein stability and the apparent unfolding behavior. |
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| 書誌情報 |
Journal of Biochemistry en : Journal of Biochemistry 巻 99, 号 4, p. 1191-1201, 発行日 1986 |
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| 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 | 3711060 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1093/oxfordjournals.jbchem.a135582 | |||||
| 関連名称 | 10.1093/oxfordjournals.jbchem.a135582 | |||||
| 権利 | ||||||
| 権利情報 | © 1986, Japanese Biochemical Society | |||||
