Thermal stability of carp G-actin monitored by loss of polymerization activity using an extrinsic fluorescent probe
Article first published online: 1 FEB 2008
© 2008 Japanese Society of Fisheries Science
Volume 74, Issue 1, pages 193–199, February 2008
How to Cite
OOI, A., YANO, F. and OKAGAKI, T. (2008), Thermal stability of carp G-actin monitored by loss of polymerization activity using an extrinsic fluorescent probe. Fisheries Science, 74: 193–199. doi: 10.1111/j.1444-2906.2007.01510.x
- Issue published online: 1 FEB 2008
- Article first published online: 1 FEB 2008
- Received 20 April 2007. Accepted 3 September 2007.
- Cyprinus carpio;
- divalent cation;
- thermal stability
ABSTRACT: The thermal stability of carp G-actin was investigated by monitoring loss of actin polymerization ability. To determine the amount of native actin remaining after heat treatment, actin was labeled with a fluorescence reagent, N-(1-pyrene)iodoacetamide. The loss of polymerization ability of carp actin during heat treatment, at between 45 and 55°C, occurred faster than that of chicken actin. The inactivation rate was influenced by concentrations of ATP and Ca2+ in solution. With the increase of Ca2+ concentration, the inactivation of carp actin was markedly suppressed. Furthermore, the activation energy of the inactivation of carp actin obtained from an Arrhenius plot was similar to that of chicken actin. These results indicated that the thermal instability of carp G-actin was due to the low affinites of ATP and Ca2+ for carp actin described in a previous report.