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

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Title: Effect of hydrostatic pressure on unfolding of α-lactalbumin: volumetric equivalence of the molten globule and unfolded state
Authors: Kobashigawa, Y. Browse this author
Sakurai, M. Browse this author
Nitta, K.3 Browse this author →KAKEN DB
Authors(alt): 新田, 勝利3
Issue Date: Dec-1999
Publisher: Cambridge University Press
Journal Title: Protein Science
Volume: 8
Issue: 12
Start Page: 2765
End Page: 2772
Abstract: 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.
Rights: Copyright © 1999 Cambridge University Press
Type: article
URI: http://hdl.handle.net/2115/7396
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 新田 勝利

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