@article{oai:ir.kagoshima-u.ac.jp:00000826,
 author = {KAMINISHI, Yoshio and MIKI, Hidemasa and NISHIMOTO, Jun-ichi},
 journal = {鹿児島大学水産学部紀要=Memoirs of Faculty of Fisheries Kagoshima University},
 month = {2016-10-27},
 note = {The effect of urea on the thermal denaturation of myosin B was investigated from
the viewpoints of aggregation process, sulfhydryl, and hydrophobic behaviors. The
degrees of turbidity and light scattering intensity decreased with increasing the urea
concentration on heating from 20 to 80°C, compared with myosin B in the absence of
urea. These phenomena suggested that the aggregation process of myosin B was
inhibited by thepresence of urea. The surface sulfhydryl groups of myosin B were
oxidized readily by heating myosin B in the presence of urea. 8-Anilino-1-naphthalenesulfonate
fluorescence intensity indicated that the amount of hydrophobic
group decreased with the increase of the oxidized SH group. These results suggested
that the configuration of myosin B molecule consequently changed to be compact
within a single myosin B on the treatment of urea and heating.},
 pages = {103--109},
 title = {Thermal Denaturation of Myosin B in the Presence of Urea},
 volume = {40},
 year = {}
}