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 degrees C, but no volume change has been found for bovine alpha-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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