Advertisement

Marine Biology

, Volume 110, Issue 1, pp 85–91 | Cite as

Metabolism of proline by the tiger prawnPenaeus esculentus

  • D. M. Smith
  • W. Dall
Article

Abstract

The distribution and fate of14C-proline were investigated in immature tiger prawns,Penaeus esculentus Haswell, collected in Moreton Bay, Cleveland, Australia, by trawling during 1986/1987. Initially the prawns were fed14C-proline in food pellets to follow the pathway of proline absorption and distribution in the body.14C-proline was also injected directly into the prawn to provide sufficient tracer to follow the incorporation of14C into other amino acids and into proteins. A comparison was made of the metabolism of injected14C-proline over 48 h in prawns that had been fed and those that had been starved for 10 d. Free amino acids (FAA) in the muscle and protein-bound amino acids were analysed separately. Labelled proline was completely absorbed and distributed within the body 3 h after ingestion, about 80% being in the tissues, mostly in muscle. There was no significant difference between the total CO2 output in fed and starved prawns, but the latter metabolised about twice the amount of labelled proline over 48 h. At this time, in abdominal muscle of fed prawns, about 95% of the total muscle label was in the FAA; of the label in the FAA, 78% was proline and 18% glutamic acid, with the remainder in hydroxyproline, aspartic acid, glutamine, alanine and Kreb's cycle intermediates. In the starved prawns, proline was 58%, glutamic acid 24%, with correspondingly higher amounts in the other compounds. In the muscle protein, the distribution of label was similar in fed and starved prawns, with 72 to 74% as proline. The experiments showed that proline is not very labile in the tiger prawn and its rate of synthesis is slow. It does not appear to be an important source of energy as in some insects and cephalopods, but during starvation is only slowly oxidised for energy.

Keywords

Proline Glutamic Acid Aspartic Acid Free Amino Acid Hydroxyproline 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literature cited

  1. Adams, E., Frank, L. (1980). Metabolism of proline and the hydroxyprolines. A. Rev. Biochem. 49: 1005–1061Google Scholar
  2. Barclay, M. C., Dall, W., Smith, D. M. (1983). Changes in lipid and protein during starvation and the moulting cycle in the tiger prawn,Penaeus esculentus Haswell. J. exp. mar. Biol. Ecol. 68: 229–244Google Scholar
  3. Brody, S. (1964). Bioenergetics and growth. Hafner Publishing Co., Darien, Connecticut, USAGoogle Scholar
  4. Claybrook, D. L. (1983). Nitrogen metabolism. In: Mantel, L. H. (ed.) The biology of Crustacea. Vol. 5. Internal anatomy and physiological regulation. Academic Press, New York, p. 163–213Google Scholar
  5. Cowey, C. B., Forster, J. R. M. (1971). The essential amino-acid requirements of the prawnPalaemon serratus. The growth of prawns on diets containing proteins of different amino-acid compositions. Mar. Biol. 10: 77–81Google Scholar
  6. Dall, W., Hill, B. J., Rothlisberg, P. C., Staples, D. J. (1990). The biology of the Penaeidae. Adv. mar. Biol. 27: 167–170Google Scholar
  7. Dall, W., Smith, D. M. (1986). Oxygen consumption and ammonia-N excretion in fed and starved tiger prawns,Penaeus esculentus Haswell. Aquaculture, Amsterdam 55: 23–33Google Scholar
  8. Dall, W., Smith, D. M. (1987). Changes in protein-bound and free amino acids in the muscle of the tiger prawnPenaeus esculentus during starvation. Mar. Biol. 95: 509–520Google Scholar
  9. Deshimaru, O., Shigeno, K. (1972). Introduction to the artificial diet for prawnPenaeus japonicus. Aquaculture, Amsterdam 1: 115–133Google Scholar
  10. Fair, P. H., Sick, L. V. (1982). Serum amino acid concentrations during starvation in the prawn,Macrobrachium rosenbergii, as an indicator of metabolic requirements. Comp. Biochem. Physiol. 73: 195–200Google Scholar
  11. Farmanfarmaian, A., Lauterio, T. (1980). Amino acid composition of the tail muscle ofMacrobrachium rosenbergii, comparison to amino acid patterns of supplemented commercial feed pellets. Proc. Wld Maricult. Soc. 11: 454–462Google Scholar
  12. Hill, B. J., Wassenberg, T. J. (1987). Feeding behaviour of adult tiger prawns,Penaeus esculentus, under laboratory conditions. Aust. J. mar. Freshwat. Res. 38: 183–190Google Scholar
  13. Hochachka, P. W., Mommsen, T. P., Storey, J., Storey, K. B., Johansen, K., French, C. J. (1983). The relationship between arginine and proline metabolism in cephalopods. Mar. Biol. Lett. 4: 1–21Google Scholar
  14. Kanazawa, A., Teshima, A., Sasada, H., Abdel Rahman, S. (1982). Culture of prawn larvae with micro-particulate diets. Bull. Jap. Soc. scient. Fish. 48: 195–199Google Scholar
  15. Marrewijk, W. J. A., van, Ravenstein, H. J. L. (1974). Amino acid metabolism ofAstacus leptodactylus Esch. I. Composition of the free and protein-bound amino acids in different organs of the crayfish. Comp. Biochem. Physiol. 47B: 531–542Google Scholar
  16. Marrewijk, W. J. A., van, Zandee, D. I. (1975). Amino acid metabolism ofAstacus leptodactylus (Esch.). II. Biosynthesis of the non-essential amino acids. Comp. Biochem. Physiol. 50B: 449–455Google Scholar
  17. Roberts, D. G., Smith, D. M. (1988). Infrared gas analysis of both gaseous and dissolved CO2 in small-volume marine samples. Limnol. Oceanogr. 33: 135–140Google Scholar
  18. Smith, D. M., Dall, W. (1982). Blood protein, blood volume and extracellular space relationships in twoPenaeus spp. (Decapoda: Crustacea). J. exp. mar. Biol. Ecol. 63: 1–15Google Scholar
  19. Taft, J. L. (1976). Recovery of14C-CO2 at high flow rates from a CHN analyser. Limnol. Oceanogr. 21: 161–164Google Scholar
  20. Torres, C. (1973). Variations du pool des acides aminés libres du muscle abdominal dePenaeus kerathurus au cours du cycle d'intermue, et au cours du jêune. Comp. Biochem. Physiol. 45: 1–12Google Scholar
  21. Weeda, E., de Kort, C. A. D., Beenakkers, A. M. T. (1980). Oxidation of proline and pyruvate by flight muscle mitochondria of the Colorado beetle,Leptinotarsa decemlineata Say. Insect Biochem. 10: 305–311Google Scholar

Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • D. M. Smith
    • 1
  • W. Dall
    • 1
  1. 1.CSIRO Marine LaboratoriesClevelandAustralia

Personalised recommendations