Effect of hydrostatic pressure on unfolding of α-lactalbumin: volumetric equivalence of the molten globule and unfolded state

Kobashigawa, Y.; Sakurai, M.; Nitta, K.

Protein Science, 1999, 8(12), 2765-2772

Permalink : https://hdl.handle.net/2115/7396

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アクセス権	open access
URI	https://hdl.handle.net/2115/7396
タイトル	Effect of hydrostatic pressure on unfolding of α-lactalbumin: volumetric equivalence of the molten globule and unfolded state
著者	Kobashigawa, Y. ; Sakurai, M. ; Nitta, K.
著者名 Kobashigawa, Y.
著者名 Sakurai, M.
e-Rad_Researcher 80001858 著者名 Nitta, K. 新田, 勝利
言語	英語
発行日	1999-12
出版者	Cambridge University Press
収録物名	Protein Science
巻(号)	8(12)
ページ	2765-2772
抄録	The effect of pressure on the unfolding of bovine alpha-lactalbumin was investigated by ultraviolet absorption methods. The change of molar volume associated with unfolding, deltaV, was measured in the presence or absence of guanidine hydrochloride at pH 7. The deltaV was estimated to be -63 cm3/mol in the absence of a chemical denaturant. While in the presence of guanidine hydrochloride (GuHCl), it was found that deltaV was -66 cm3/mol at 25 degrees C and was independent of the concentration of GuHCl, despite the fact that the molten globule fraction in the total unfolding product decreased with the increase of GuHCl concentration. The results indicate that the volume of alpha-lactalbumin only changes at the transition from a native to a molten globule state, and almost no volume change has been found during the transition from a molten globule to the unfolded state.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
権利情報	Copyright © 1999 Cambridge University Press
PISSN	0031-1820