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Evolutionary adaptation to temperature in fish muscle cross bridge mechanisms: tension and ATP turnover

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Summary

  1. 1.

    Force and ATPase activity were measured in skinned, fast muscle fibres isolated from the myotomes of Antarctic, temperate and tropical fish.

  2. 2.

    Maximum isometric tension was inversely related to normal environmental temperature, when measured at −5 to 0°C. When compared within the normal temperature range of each species, tensions were rather similar.

  3. 3.

    In contrast, the muscle fibres of all three species had similar cross bridge cycle times over the entire temperature range studied. This results in a more economical maintenance of force at normal body temperatures in muscle fibres from the Antarctic fish.

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References

  • Altringham JD, Johnston IA (1985) Adenosine triphosphatase measurements in skinned muscle fibres using high performance liquid chromatography. J Physiol 367:6P

    Google Scholar 

  • Altringham JD, Johnston IA (1986) The energy cost of contraction in fast and slow skinned muscle fibres isolated from an elasmobranch and an Antarctic teleost fish. J Exp Biol 121:239–250

    Google Scholar 

  • Connell JJ (1960) Studies on the proteins of fish skeletal muscle. 7. Denaturation and aggregation of cod myosin. Biochem J 75:530–538

    Google Scholar 

  • Connell JJ (1961) The relative stabilities of skeletal muscle myosins of some animals. Biochem J 80:503–509

    Google Scholar 

  • Ferenczi MA, Homsher E, Simmons RM, Trenthan DR (1978) Reaction mechanism of the magnesium ion-dependent adenosine triphosphatase of frog muscle myosin and subfragment-1. Biochem J 171:165–175

    Google Scholar 

  • Johnston IA, Altringham JD (1985) Evolutionary adaptation of muscle power output to enviromental temperature: force-velocity characteristics of skinned fibres isolated from Antarctic, temperate and tropical marine fish. Pflügers Arch 405:136–140

    Google Scholar 

  • Johnston IA, Brill R (1984) Thermal dependence of contractile properties of single skinned muscle fibres isolated from Antarctic and various Pacific marine fishes. J Comp Physiol B 155:63–70

    Google Scholar 

  • Johnston IA, Mutungi G (1985) Effects of pH and temperature on the contractile properties of skeletal muscle fibres isolated from the iliofibularis muscle of the freshwater turtle,Pseudemys scripta elegans. J Physiol 367:79P

    Google Scholar 

  • Johnston IA, Walesby NJ (1977) Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases. J Comp Physiol 119:195–206

    Google Scholar 

  • Johnston IA, Walesby NJ, Davison W, Goldspink G (1975) Temperature adaptation in myosin of Antarctic fish. Nature 254:74–75

    Google Scholar 

  • Shriver JW (1984) Energy transduction in myosin. Trends Biochem Sci 9:322–327

    Google Scholar 

  • Somero GN, DeVries AL (1967) Temperature tolerance of some Antarctic fishes. Science 156:257–258

    Google Scholar 

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Authors and Affiliations

  1. Gatty Marine Laboratory and Department of Physiology, University of St. Andrews, KY16 8LB, Fife, Scotland

    J. D. Altringham & I. A. Johnston

Authors
  1. J. D. Altringham
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  2. I. A. Johnston
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Altringham, J.D., Johnston, I.A. Evolutionary adaptation to temperature in fish muscle cross bridge mechanisms: tension and ATP turnover. J Comp Physiol B 156, 819–821 (1986). https://doi.org/10.1007/BF00694256

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  • DOI: https://doi.org/10.1007/BF00694256

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