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Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human α-Lactalbumin by Circular Dichroism Spectroscopy
https://ir.soken.ac.jp/records/4298
https://ir.soken.ac.jp/records/429834837f86-6df0-40d4-8799-2597917a0aed
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-14 | |||||
| タイトル | ||||||
| タイトル | Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human α-Lactalbumin by Circular Dichroism Spectroscopy | |||||
| タイトル | ||||||
| タイトル | Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human α-Lactalbumin by Circular Dichroism Spectroscopy | |||||
| 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 |
CHAUDHURI, Tapan K
× CHAUDHURI, Tapan K× KUWAJIMA, Kunihiro× et, al. |
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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 | The equilibrium and kinetics of the unfolding and refolding of authentic and recombinant human α-lactalbumin, the latter of which had an extra methionine residue at the N-terminus, were studied by circular dichroism spectroscopy, and the results were compared with the results for bovine and goat α-lactalbumins obtained in our previous studies. As observed in the bovine and goat proteins, the presence of the extra methionine residue in the recombinant protein remarkably destabilized the native state, and the destabilization was entirely ascribed to an increase in the rate of unfolding. The thermodynamic stability of the native state against the unfolded state was lower, and the thermodynamic stability of the molten globule state against the unfolded state was higher for the human protein than for the other α-lactalbumins previously studied. Thus, the population of the molten globule intermediate was higher during the equilibrium unfolding of human α-lactalbumin by guanidine hydrochloride. Unlike the molten globule states of the bovine and goat proteins, the human α-lactalbumin molten globule showed remarkably more intense circular dichroism ellipticity than the native state in the far-ultraviolet region below 225 nm. During refolding from the unfolded state, human α-lactalbumin thus exhibited overshoot kinetics, in which the α-helical peptide ellipticity exceeded the native value when the molten globule folding intermediate was formed in the burst phase. The subsequent folding involved reorganization of nonnative secondary structures. It should be noted that the rate constant of the major refolding phase was approximately the same among the three types of α-lactalbumin and that the rate constant of unfolding was accelerated 18−600 times in the human protein, and these results interpreted the lower thermodynamic stability of this protein. | |||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 39, 号 50, p. 15643-15651, 発行日 2000 |
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| 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 | 0006-2960 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | http://doi.org/10.1021/bi001735j | |||||
| 関連名称 | 10.1021/bi001735j | |||||
| 権利 | ||||||
| 権利情報 | © 2000 American Chemical Society | |||||
