Skip to main content

Temperature adaptation in enzymes of antarctic fish

  • Chapter
Cold-Adapted Organisms

Abstract

The study of the biochemical basis underlying the adaptation processes to different environments yields important information when investigating organisms living under extreme conditions. Antarctic organisms are a precious tool to investigate molecular properties acquired during adaptation to the lowest temperatures in the world. Antarctic fish are a taxonomically uniform group of teleosts, which evolved in geographic and climatic isolation and live at −1.97°C throughout the year. Because of the constant temperature of the seawater they developed a high degree of stenothermality and were defined as a paradox in being ectothermic homeotherms.1 In fact, antarctic species such as Pagothenia borchgrevinki, Trematomus bernacchii and Trematomus hansoni do not survive at temperatures of only a few degrees higher than that of the habitat.2 Due to their unique ecological characteristics, antarctic fish show unusual features. One of the most significant evolutionary trends is the decrease in erythrocyte number and hemoglobin concentration in their blood,3,4 possibly reaching the extreme stage in the hemoglobin-less family Channichthyidae (icefish),5 whose blood is virtually devoid of erythrocytes.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Macdonald JA, Montgomery JC, Wells RMG. Comparative physiology of Antarctic fishes. Adv Mar Biol 1987; 24: 321–387.

    Article  Google Scholar 

  2. Somero GN, DeVries AL. Temperature tolerance of some Antarctic fishes. Science 1967; 156: 257–258.

    Article  CAS  Google Scholar 

  3. Everson I, Ralph R. Blood analyses of some Antarctic fish. Br Antarctic Sury Bull 1968; 15: 5962.

    Google Scholar 

  4. Wells RMG, Ashby MD, Duncan SJ, Macdonald JA. Comparative study of the erythrocytes and hemoglobins in nototheniid fishes from Antarctica. J Fish Biol 1980; 17: 517–527.

    Article  Google Scholar 

  5. Ruud JT. Vertebrates without erythrocytes and blood pigments. Nature 1954; 173: 848–850.

    Article  CAS  Google Scholar 

  6. Somero GN, Hochachka PW. The effect of temperature on catalytic and regulatory functions of pyruvate kinases of the rainbow trout and the Antarctic fish Trematomus bernacchii. Biochem J 1968; 110: 395–400.

    CAS  Google Scholar 

  7. Feeney RE, Osuga DT. Blood proteins and muscle enzymes of cold-adapted antarctic fishes. In: Quam LO, ed. Research in the Antarctic. Am Assoc Adv Sci, Washington DC, 1971: 227257.

    Google Scholar 

  8. Feller G, Payan F, Theys F, Qian M, Haser R, Gerday C. Stability and structural analysis of a-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem 1994; 222: 441–447.

    Article  CAS  Google Scholar 

  9. Genicot S, Feller G, Gerday C. Trypsin from Antarctic fish (Paranotothenia magellanica Forster) as compared with the trout (Salmo gairdneri) trypsin. Comp Biochem Physiol 1988; 90B: 601–609.

    Google Scholar 

  10. Davail S, Feller G, Narinx E, Gerday C. Cold adaptation of proteins. Purification, characterisation and sequence of heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. J Biol Chem 1994; 269: 17448–17453.

    CAS  Google Scholar 

  11. Ciardiello MA, Camardella L Carratore V, di Prisco G. Enzymes in Antarctic fish: glucose-6phosphate dehydrogenase and glutamate dehydrogenase. Comp Biochem Physiol 1997; 118A: 1031–1036.

    Article  CAS  Google Scholar 

  12. Ciardiello MA, Camardella L, di Prisco G. Enzymes in cold-adapted Antarctic fish: Glucose6-phosphate dehydrogenase. In: Battaglia B, Valencia J, Walton H, eds. Proc 6th SCAR Biol Symp, Antarctic Communities: Species, Structure and Survival. Cambridge: Cambridge Univ Press; 1997: 261–265.

    Google Scholar 

  13. di Prisco G, D’Avino R. Molecular adaptation of the blood of Antarctic teleosts to environmental conditions. Antarctic Sci 1989; 1: 119–124.

    Article  Google Scholar 

  14. Hemmingsen EA, Douglas EL. Respiratory and circulatory adaptation to the absence of hemoglobin in Channichthyid fishes. In: Llano GA, ed. Adaptation within Antarctic Ecosystems. Washington, DC: Smithsonian Institution, 1977: 479–487.

    Google Scholar 

  15. Feller G, Narinx E, Arpigny JL, Aittaleb M, Baise E, Genicot S, Gerday C. Enzymes from psychrophilic organisms. FEMS Microbiol Rev 1996; 18: 189–202.

    Article  CAS  Google Scholar 

  16. Ciardiello MA, Camardella L, di Prisco G. Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: correlation with cold adaptation. Biochim Biophys Acta 1995; 1250: 76–82.

    Article  Google Scholar 

  17. Ciardiello MA, Camardella L, di Prisco G. Enzymes of Antarctic fishes: effect of temperature on catalysis. Cybium 1997; 21: 443–450.

    Google Scholar 

  18. Hochachka PW, Somero GN. Biochemical Adaptations. New Jersey: Princeton Univ Press; 1984.

    Google Scholar 

  19. Somero GN. Biochemical mechanisms of cold adaptation and stenothermality in Antarctic fish. In: di Prisco G, Maresca B, Tota B, eds. Biology of Antarctic Fish. Heidelberg: Springer, 1991: 232–247.

    Chapter  Google Scholar 

  20. Feller G, Pauly J-P, Smal A, O’Carra P, Gerday C. The lactate dehydrogenase of the icefish heart: biochemical adaptations to hypoxia tolerance. Biochim Biophys Acta 1991; 1079: 343347.

    Google Scholar 

  21. Low PS, Bada JL, Somero GN. Temperature adaptation of enzymes: roles of the free energy, the enthalpy and the entropy of activation. Proc Natl Acad Sci USA 1973; 70: 430–432.

    Article  CAS  Google Scholar 

  22. Detrich HW III. Polymerization of microtubule proteins from Antarctic fish. In: di Prisco G, Maresca B, Tota B, eds. Biology of Antarctic Fish. Berlin: Springer, 1991: 248–262.

    Chapter  Google Scholar 

  23. Veronese FM, Bevilacqua R, Bocci]. E, Brown DM. Glutamate dehydrogenase from tuna liver. Purification, characteristics and sequence of a peptide containing an essential lysine residue. Biochim Biophys Acta 1976; 445: 1–13.

    Article  CAS  Google Scholar 

  24. Corman L, Prescott LM, Kaplan NO. Purification and kinetic characteristics of dogfish liver glutamate dehydrogenase. J Biol Chem 1966; 242: 1383–1390.

    Google Scholar 

  25. Gerike U, Danson MJ, Russell NJ, Hough DW. Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2–3R. Eur J Biochem 1997; 248: 49–57.

    Article  CAS  Google Scholar 

  26. Benachenhou-Lahfa N, Forterre P, Labedan B. Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archeobacteria in the universal tree of life. J Mol Evol 1993; 36: 335–346.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to G. di Prisco .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1999 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Ciardiello, M.A., Camardella, L., di Prisco, G. (1999). Temperature adaptation in enzymes of antarctic fish. In: Margesin, R., Schinner, F. (eds) Cold-Adapted Organisms. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-06285-2_16

Download citation

  • DOI: https://doi.org/10.1007/978-3-662-06285-2_16

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-08445-4

  • Online ISBN: 978-3-662-06285-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics