@article{oai:tsukuba.repo.nii.ac.jp:00029510,
 author = {白木, 賢太郎 and 白木, 賢太郎},
 journal = {International journal of biological macromolecules},
 month = {Oct},
 note = {Myosin is an important protein resource for food industries and has a bipolar filamentous structure that is composed of subfilaments that occur in vivo. It has been shown that a high ionic strength is required to prevent myosin from forming filamentous structures and to solubilize the protein in aqueous solution. In the presence of 100–200 mM NaCl, 50 mM arginine was more effective than other additives tested, including NaCl, in myosin solubilization. Before reaching equilibrium solubility, the myosin solution was initially supersaturated upon the dilution of a stock myosin solution in 1 M NaCl into the test solvents. Arginine slowed the process of equilibration and stabilized the supersaturated solution more effectively than other additives. No structural changes in myosin caused by arginine were observed, which indicated that arginine enhanced the solubility of myosin in a physiological salt solution without affecting the structure.},
 pages = {647--651},
 title = {Synergistic solubilization of porcine myosin in physiological salt solution by arginine},
 volume = {62},
 year = {2013},
 yomi = {シラキ, ケンタロウ}
}