Stabilization of myosin by ionic compounds as affected by F-actin |
| |
| Authors: | Kumiko Hayashi Kunihiko Konno |
| |
| Institution: | Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan |
| |
| Abstract: | ABSTRACT: Suppressive effects of non-ionic (sorbitol, maltose, and trehalose) and ionic (Na-glutamate, Na-acetate, Na-sulfate, and ammonium sulfate) compounds on the thermal inactivation of myosin subframgent-1 (S-1) and myofibril Ca2+-ATPase were compared. All compounds suppressed S-1 denaturation. When myofibrils were used (at 0.1 M KCl), sugars and sugar alcohol (non-ionic compounds) suppressed denaturation similar to S-1, while Na-glutamate, Na-acetate, and Na-sulfate weakly suppressed them. Ammonium sulfate accelerated denaturation, but suppressed denaturation when heated in 2 M KCl, at which myosin lost protection by F-actin. It was thus concluded that ionic compounds affected the denaturation of myofibrils in two ways; suppression as established with S-1, and acceleration as a result of loss of protection by F-actin caused by increase in ionic strength. |
| |
| Keywords: | amino acid myosin sugar suppression of denaturation thermal denaturation |
| 本文献已被 SpringerLink 等数据库收录！ |
|
