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Marine Biology

, Volume 112, Issue 3, pp 363–369 | Cite as

Nucleic acid concentrations and enzyme activities as correlates of growth rate of the saithe Pollachius virens: growth-rate estimates of open-sea fish

  • E. M. Mathers
  • D. F. Houlihan
  • M. J. Cunningham
Article

Abstract

The aim of this study was to estimate the growth rate of saithe, Pollachius virens L., in wild populations collected from around the Beryl Alpha oil platform in October 1988 and from Loch Ewe on the west coast of Scotland in August 1989, by comparing the concentrations of various growth-rate indicators in the white muscle with those of laboratory-maintained individuals of known growth rates. There were significant correlations between the individual growth rates of laboratory-maintained saithe and concentrations of white muscle RNA expressed as μg RNA mg-1 protein, mg RNA mg-1 DNA and as mg RNA g-1 muscle. Growth rate was also correlated with the activities of the enzymes citrate synthase, cytochrome oxidase and lactate dehydrogenase. RNA concentrations decreased with increasing body size, and weight-corrected estimates of RNA concentrations for a standard-sized individual were determined from the scaling relationships. RNA concentrations expressed in three different ways gave similar estimates of the growth rate for two samples of wild saithe, one from around an oil platform and the other from the west coast of Scotland. RNA concentrations were correlated with aerobic enzyme levels in oil-platform fish, although the growth rate estimates of the same wild fish were lower when expressed as a function of aerobic enzyme levels than when expressed as a function of lactate dehydrogenase concentration. It is concluded that the capacity for protein synthesis of white muscle expressed as RNA concentrations in relation to wet or dry weight may be used as an estimate of instantaneous growth rate and that additional confidence in such estimates may be gained from measurement of the levels of aerobic enzymes.

Keywords

Cytochrome Oxidase White Muscle Largemouth Bass Wild Fish Nucleic Acid Concentration 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Literature cited

  1. Alp, P. R., Newsholhme, E. A., Zamit, V. A. (1976). Activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenase in muscle from vertebrates and invertebrates. Biochem. J 154:689–700Google Scholar
  2. Buckley, L. J. (1979). Relationships between RNA-DNA ratio, prey density and growth rate in Atlantic cod, Gadus morhua, larvae. J. Fish. Res. Bd Can. 36:1497–1502CrossRefGoogle Scholar
  3. Buckley, L. J. (1982). Effects of temperature on growth and biochemical composition of larval winter flounder, Pseudopleuronectes americanus. Mar. Ecol. Prog. Ser. 8:181–186CrossRefGoogle Scholar
  4. Buckley, L. J. (1984). RNA-DNA ratio: an index of larval fish growth in the sea. Mar. Biol. 80:291–298CrossRefGoogle Scholar
  5. Buckley, L. J., Lough, R. G. (1987). Recent growth, biochemical composition and prey field of larval haddock, Melanogrammus aeglefinus and Atlantic cod, Gadus morhua on Georges Bank. Can. J. Fish. aquat. Sciences 44:14–25CrossRefGoogle Scholar
  6. Bulow, F. J. (1970). RNA-DNA ratios as indicators of recent growth rates of a fish. J. Fish. Res. Bd Can. 27:2343–2349CrossRefGoogle Scholar
  7. Bulow, F. J. (1987). RNA:DNA ratios as indicators of growth in fish. In: Summerfelt, R. C., Hall, G. E. (eds.) Age and growth of fish. Iowa State University Press, Ames, Iowa, p. 45–64Google Scholar
  8. Campana, S. E., Hurley, P. C. F. (1989). An age-and temperature-mediated growth model for cod, Gadus morhua, and haddock, Melanogrammus aeglefinus larvae in the Gulf of Maine. Can. J. Fish. aquat. Sciences 46:603–613CrossRefGoogle Scholar
  9. Childress, J. J., Somero, G. N. (1990). Metabolic scaling: a new perspective on scaling of glycolytic enzyme activities. Am. Zool. 30: 161–173Google Scholar
  10. Downs, T., Wilfinger, W. W. (1983). Fluorometric quantification of DNA in cells and tissues. Analyt. Biochem 131:538–547CrossRefGoogle Scholar
  11. Ewart, H. S., Canty, A. A., Dreidzic, W. R. (1988). Scaling of cardiac oxygen consumption and enzyme activity levels in the sea raven (Hemitripterus americanus). Physiol. Zoöl. 61:50–56Google Scholar
  12. Foster, A. R. (1990). Growth and protein turnover in fish. Ph. D. thesis. University of AberdeenGoogle Scholar
  13. Goolish, E. M., Adelman, I. R. (1987). Tissue-specific cytochrome oxidase activity in largemouth bass: the metabolic costs of feeding and growth. Physiol. Zoöl. 69:454–464Google Scholar
  14. Goolish, E. M., Adelman, I. R. (1988). Tissue-specific allometry of an aerobic respiratory enzyme in a large and small species of cyprinid (Teleostei). Can. J. Zool. 66:2199–2208CrossRefGoogle Scholar
  15. Goolish, E. M., Barron, M. G., Adelman, I. R. (1984). Thermoacclimatory response of nucleic acid and protein content of carp muscle tissue: influence of growth rate and relationship to glycine uptake by scales. Can. J. Zool. 62:2164–2170CrossRefGoogle Scholar
  16. Haines, T. A. (1973). An evaluation of RNA-DNA ratio as a measure of long-term growth in fish populations. J. Fish. Res. Bd Can. 30:195–199CrossRefGoogle Scholar
  17. Hansen, C. A., Sidell, B. D. (1983). Atlantic hagfish cardiac muscle: metabolic basis of tolerance to anoxia. Am. J. Physiol. 244: R356–362Google Scholar
  18. Houlihan, D. F. (1991). Protein turnover in ectotherms and its relationship to energetics. In: Gilles, R. (ed.) Advances in comparative and environmental physiology. Vol. 7. Springer-Verlag, Berlin Heidelberg, p. 1–43CrossRefGoogle Scholar
  19. Houlihan, D. F., Hall, S. J., Gray, C. (1989). Effects of protein turnover in cod. Aquaculture, Amsterdam 79:103–110CrossRefGoogle Scholar
  20. Houlihan, D. F., McMillan, D. N., Agnisola, C., Trara Genoino, I., Foti, L. (1990a). Protein synthesis and growth in Octopus vulgaris. Mar. Biol. 106:251–259CrossRefGoogle Scholar
  21. Houlihan, D. F., McMillan, D. N., Laurent, P. (1986). Growth rates, protein synthesis and protein degradation rates in rainbow trout: effects of body size. Physiol. Zoöl. 59:482–493Google Scholar
  22. Houlihan, D. F., Waring, C. P., Mathers, E., Gray, C. (1990b). Protein synthesis and oxygen consumption of the shore crab Carcinus maenas after a meal. Physiol. Zoöl. 63:735–756Google Scholar
  23. Jobling, M. (1983). Growth studies with fish — overcoming the problems of size variation. J. Fish. Biol. 22:153–157CrossRefGoogle Scholar
  24. Kent, J., Koban, M., Ladd Proser, C. (1988). Cold-acclimation-induced protein hypertrophy in channel catfish and green sunfish. J. comp. Physiol. (Sect. B) 158:185–198CrossRefGoogle Scholar
  25. Loughna, P. T., Goldspink, G. (1984). The effects of starvation upon protein turnover in red and white myotomal muscle of rainbow trout, Salmo gairdneri Richardson. J. Fish Biol. 25: 223–230CrossRefGoogle Scholar
  26. Lowery, M. S., Roberts, S. J., Somero, G. N. (1987). Effects of starvation on the activities and localisation of glycolytic enzymes in the white trunk muscle of the barred sand bass, Paralabrax nebulifer. Physiol. Zoöl. 60:538–549Google Scholar
  27. M. A. F. F. (1981). Atlas of the seas around the British Isles. Ministry of Agriculture, Fisheries and Food, Southampton, EnglandGoogle Scholar
  28. McMillan, D. N., Houlihan, D. F. (1988). The effects of refeeding on tissue protein synthesis in rainbow trout. Physiol. Zoöl. 61: 429–441Google Scholar
  29. Millward, D. J., Garlick, P. J., James, W. P. T., Nnanyelugo, D. O., Ryatt, J. S. (1973). Relationships between protein systhesis and RNA content in skeletal muscle. Nature, Lond 241:204–205CrossRefGoogle Scholar
  30. Moon, T. W., Johnston, I. A. (1980). Starvation and the activities of glycolytic and gluconeogenic enzymes in the skeletal muscles and liver of the plaice, Pleuronectes platessa. J. comp. Physiol. 136:31–38CrossRefGoogle Scholar
  31. Pain, V. M., Clemens, M. J. (1980). Protein synthesis in mammalian systems. In: Florkin, M., Neuberger, A., van Deenen, L. L. M. (eds.) Protein metabolism 19B(1), Elsevier, Amsterdam, p. 1–76Google Scholar
  32. Preedy, V. R., Paska, L., Sugden, P. H., Schofield, P. S., Sugden, M. C. (1988). The effects of surgical stress and short term fasting on protein synthesis in vivo in diverse tissues of the mature rat. Biochem. J. 250:179–188Google Scholar
  33. Ricker, W. E. (1973). Linear regressions in fishery research. J. Fish. Res. Bd Can. 30:409–434CrossRefGoogle Scholar
  34. Ricker, W. E. (1979). Growth rates and models. In: Hoar, W. S., Randall, D. J., Brett, J. R. (eds.) Fish physiology. Vol. 8. Academic Press, New York, p. 677–743Google Scholar
  35. Robinson, S. M. C., Ware, D. M. (1988). Ontogenetic development of growth rates in larval Pacific herring, Clupea harengus pallasi, measured with RNA:DNA ratios in the Strait of Georgia, British Columbia. Can. J. Fish. aquat. Sciences 45:1422–1429CrossRefGoogle Scholar
  36. Somero, G. N., Childress, J. J. (1980). A violation of the metabolismsize scaling paradigm: activities of glycolytic enzymes in muscle increase in larger-size fish. Physiol Zoöl. 53:322–337Google Scholar
  37. Sullivan, K. M., Somero, G. (1983). Size-and diet-related variations in enzymatic activity and tissue composition in the sablefish, Anoplopoma fimbria. Biol. Bull. mar. biol. Lab., Woods Hole 164:315–326CrossRefGoogle Scholar
  38. Torres, J. J., Somero, G. N. (1988). Metabolism, enzymic activities and cold adaptation in Antarctic mesopelagic fishes. Mar. Biol. 98:169–180CrossRefGoogle Scholar
  39. Zar, J. H. (1974). Biostatistical analysis. Prentice-Hall, Englewood Cliffs, New JerseyGoogle Scholar

Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • E. M. Mathers
    • 1
  • D. F. Houlihan
    • 2
  • M. J. Cunningham
    • 1
  1. 1.Aberdeen University Marine Studies Ltd.AberdeenScotland
  2. 2.Department of ZoologyUniversity of AberdeenAberdeenScotland

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