The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish
- 1 August 1973
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 133 (4) , 735-738
- https://doi.org/10.1042/bj1330735
Abstract
1. Myofibrillar adenosine triphosphatase (ATPase) activities were measured for white myotomal muscle of 19 species of fish. 2. The activity was measured at different temperatures and after periods of preincubation at 37°C. 3. The inactivation half-life at 37°C depended on environmental temperature, increasing as the temperature increased. 4. Cold-water fish had higher myofibrillar adenosine triphosphatase activity at low temperatures than had warm-water fish. 5. The significance of these results is discussed.Keywords
This publication has 9 references indexed in Scilit:
- Myofibrillar ATPase activities of red and white myotomal muscles of marine fishCellular and Molecular Life Sciences, 1972
- Properties of muscle glyceraldehyde-3-phosphate dehydrogenase from the cold-adapted antarctic fish Dissostichus mawsoniBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- Chromatography of Myosin on Diethylaminoethyl-Sephadex A-50*Biochemistry, 1967
- The temperature dependence of myosin-adenosinetriphosphatase and alkaline phosphatase in lizardsComparative Biochemistry and Physiology, 1964
- The relative stabilities of the skeletal-muscle myosins of some animalsBiochemical Journal, 1961
- Studies on the proteins of fish skeletal muscle. 7. Denaturation and aggregation of cod myosinBiochemical Journal, 1960
- The isolation and properties of fish myosinBiochimica et Biophysica Acta, 1959
- A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphataseBiochemical Journal, 1956
- The estimation of phosphorusBiochemical Journal, 1940