Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases

• Published in: Journal of Comparative Physiology ? B
• Main Authors: Johnston, Ian A., Walesby, N.J.
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Springer 1977
• Subjects: Antarctic; Antarc*
• Online Access: http://nora.nerc.ac.uk/id/eprint/525564/; https://doi.org/10.1007/BF00686565

Studies have been carried out on the Mg2+ Ca2+-myofibrillar ATPase from the muscles of fish adapted to different environmental temperatures. The thermal stability of the ATPase is strongly correlated with mean habitat temperature. Activities of Antarctic fish ATPases are significantly higher at low temperatures than those of temperate and tropical water species. The effects of ionic strength on ATPase activity have also been studied. The Gibbs free energy of activation (ΔG#) was found to increase and enzyme activity decrease with increasing ionic strength within the physiological temperature range of each species. Significantly lower values of ΔG#, of around 1 Kcal/mole, are obtained for the ATPase of cold-adapted compared to tropical fish. Enthalpic and entropic activation energies were also reduced in the cold adapted ATPases. It is postulated that the reduction of the enthalpic activation term in the cold adapted enzyme confers the advantage of reducing the temperature sensitivity of the rate limiting step thus partly compensating for the low heat content of the cellular environment. Possible molecular mechanisms of temperature compensation in fish myofibrillar ATPase are discussed.