Abstract
The effect of pressure on the unfolding of the molten globule (MG) state of canine milk lysozyme (CML) was examined using ultraviolet spectroscopy. The volume changes of the MG-unfolded-state transition were observed at pH 2.0 and around 20 to 60°C, but no volume change has been found for bovine α-lactalbumin, which is homologous to CML. Our results suggest that the MG state of CML possesses a tightly packed hydrophobic core.
Keywords: canine milk lysozyme, olding, hydration
Protein & Peptide Letters
Title: Volumetric Behavior of the Molten Globule State of Canine Milk Lysozyme
Volume: 11 Issue: 4
Author(s): Masahiro Watanabe, Yoshihiro Kobashigawa, Tomoyasu Aizawa, Makoto Demura and Katsutoshi Nitta
Affiliation:
Keywords: canine milk lysozyme, olding, hydration
Abstract: The effect of pressure on the unfolding of the molten globule (MG) state of canine milk lysozyme (CML) was examined using ultraviolet spectroscopy. The volume changes of the MG-unfolded-state transition were observed at pH 2.0 and around 20 to 60°C, but no volume change has been found for bovine α-lactalbumin, which is homologous to CML. Our results suggest that the MG state of CML possesses a tightly packed hydrophobic core.
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Cite this article as:
Watanabe Masahiro, Kobashigawa Yoshihiro, Aizawa Tomoyasu, Demura Makoto and Nitta Katsutoshi, Volumetric Behavior of the Molten Globule State of Canine Milk Lysozyme, Protein & Peptide Letters 2004; 11 (4) . https://dx.doi.org/10.2174/0929866043406832
DOI https://dx.doi.org/10.2174/0929866043406832 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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