2024-03-28T17:53:44Z
https://tsukuba.repo.nii.ac.jp/oai
oai:tsukuba.repo.nii.ac.jp:00029510
2022-04-27T08:58:00Z
117:306
3:62:5591:1064
Synergistic solubilization of porcine myosin in physiological salt solution by arginine
白木, 賢太郎
白木, 賢太郎
シラキ, ケンタロウ
© 2013 Elsevier B.V. NOTICE: this is the author’s version of a work that was accepted for publication in International Journal of Biological Macromolecules. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in International Journal of Biological Macromolecules, 62, 2013, http://dx.doi.org/10.1016/j.ijbiomac.2013.09.035.
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.
ELSEVIER
2013-10
eng
journal article
http://hdl.handle.net/2241/120870
https://tsukuba.repo.nii.ac.jp/records/29510
24095712
10.1016/j.ijbiomac.2013.09.035
0141-8130
AA1153092X
International journal of biological macromolecules
62
647
651
https://tsukuba.repo.nii.ac.jp/record/29510/files/IJBM_62.pdf
application/pdf
2.4 MB
2014-05-09