Volumetric behavior of the molten globule state of canine milk lysozyme.
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.
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Masahiro
M
Watanabe
Yoshihiro
Y
Kobashigawa
Tomoyasu
T
Aizawa
Makoto
M
Demura
Katsutoshi
K
Nitta
D000818:Animals; D002417:Cattle; D004285:Dogs; D057927:Hydrophobic and Hydrophilic Interactions; D007768:Lactalbumin / Q000737:chemistry / Q000378:metabolism; D008892:Milk / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D007768:Lactalbumin; D009113:Muramidase