Journal of comparative physiology

, Volume 114, Issue 2, pp 143–155 | Cite as

Responses ofMytilus edulis L. to low oxygen tension: Anaerobic metabolism of the posterior adductor muscle and mantle tissues

  • D. R. Livingstone
  • B. L. Bayne
Article

Summary

  1. 1.

    Alanine, malate and succinate accumulated in the posterior adductor muscle ofMytilus edulus L. held at the reduced oxygen tensions of 120 mm and 83 mm Hg (Figs. 2–4). The accumulations of alanine and malate were greater at the lower of the two oxygen tensions.

     
  2. 2.

    Glutamate also accumulated in the posterior adductor muscle (Fig. 1).

     
  3. 3.

    The time course of the accumulation and decline of substrates paralleled that of the physiological acclimation ofMytilus to low oxygen tensions (see Bayne and Livingstone, 1977).

     
  4. 4.

    Alanine and glutamate did not accumulate in the mantle tissues at the reduced oxygen tensions (Table 1).

     
  5. 5.

    No qualitative or quantitative changes were seen in the activities of the enzyme pyruvate kinase and PEP-carboxykinase from the posterior adductor muscle and mantle tissues, during exposure to low oxygen tension.

     

Keywords

Oxygen Enzyme Glutamate Adductor Muscle Pyruvate 
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.

Abbreviations

PEP

phosphoenolpyruvate

EDTA

ethylene diamine tetra-acetic acid

IDP

inosine-5′-diphosphate

PK

pyruvate kinase

PEPCK

PEP-carboxykinase

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Barnes, H., Blackstock, J.: The separation and estimation of free amino acids, trimethylamine oxide, and betaine in tissues and body fluids of marine invertebrates. J. exp. mar. Biol. Ecol.16, 29–45 (1974)Google Scholar
  2. Bayne, B.L.: Ventilation, the heart beat and oxygen uptake byMytilus edulis L. in declining oxygen tension. Comp. Biochem. Physiol.40A, 1065–1085 (1971a)Google Scholar
  3. Bayne, B.L.: Oxygen consumption by three species of lamellibranch mollusc in declining ambient oxygen tension. Comp. Biochem. Physiol.40A, 955–970 (1971b)Google Scholar
  4. Bayne, B.L.: The response of three species of bivalve molluse to declining oxygen tension at reduced salinity. Comp. Biochem. Physiol.45A, 793–806 (1973)Google Scholar
  5. Bayne, B.L.: Aspects of physiological condition inMytilus edulis L., with special reference to the effects of oxygen tension and salinity. In: Proc. 9th Europ. mar. biol. Symp. (H. Barnes, ed.), pp. 213–238. Aberdeen: Aberdeen University Press 1975Google Scholar
  6. Bayne, B.L., Bayne, C.J., Carefoot, T.C., Thompson, R.J.: The physiological ecology ofMytilus californianus Conrad. 2. Adaptations to low oxygen tension and air exposure. Oecologia (Berl.)22, 229–250 (1976)Google Scholar
  7. Bayne, B.L., Livingstone, D.R.: Responses ofMytilus edulis L. to low oxygen tension: Acclimation of the rate of oxygen consumption. J. comp. Physiol.114, 129–142 (1977)Google Scholar
  8. Bernt, E., Bergmeyer, H.U.: Substrates involved in protein metabolism. In: Methods in enzymatic analysis, Sect. III (H.U. Bergmeyer, ed.), pp. 384–388. New York: Academic Press 1965Google Scholar
  9. Bücher, T., Pfleiderer, G.: Enzymes of carbohydrate metabolism. In: Methods in enzymology, Vol. I, Sect. II (S.P. Colowick, N.O. Kaplan, eds.), pp. 435. New York: Academic Press 1959Google Scholar
  10. Crenshaw, M.A., Neff, J.M.: Decalcification at the mantle-shell interface in molluscs. Amer. Zool.9, 881–885 (1969)Google Scholar
  11. Dam, L. van: On the utilization of oxygen ofMya arenaria. J. exp. Biol.12, 86–94 (1935)Google Scholar
  12. Falkowski, P.G.: Facultative anaerobiosis inLimulus polyphemus: Phosphoenolpyruvate carboxykinase and heart activities. Comp. Biochem. Physiol.49B, 749–759 (1974)Google Scholar
  13. Gäde, G., Wilps, H., Kluytmans, J.H.F.M., Zwaan, A. de: Glycogen degradation and end products of anaerobic metabolism in the fresh water bivalveAnodonta cygnea. J. comp. Physiol.140, 79–85 (1975)Google Scholar
  14. Grove, W.E., Davies, F.C., Sells, B.H.: Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Analyt. Biochem.22, 195 (1968)Google Scholar
  15. Hammen, C.S.: Metabolism of the oysterCrassostrea virginica. Amer. Zool.9, 309–318 (1969)Google Scholar
  16. Hochachka, P.W.: In: Comparative animal physiology (C.L. Prosser, ed.), pp. 212–278. Philadelphia: W.B. Saunders Company 1973Google Scholar
  17. Hochachka, P.W.: Enzymatic adaptations to deep sea life. In: The biology of the Oceanic Pacific (C.B. Miller, ed.), pp. 107–136. Oregon State University Press 1974Google Scholar
  18. Hochachka, P.W., Mustafa, T.: Invertebrate facultative anaerobiosis. Science178, 1056–1060 (1972)Google Scholar
  19. Hochachka, P.W., Somero, G.N.: Strategies of biochemical adaptation. Philadelphia: W.B. Saunders Company 1973Google Scholar
  20. Hochachka, P.W., Fields, J., Mustafa, T.: Animal life without oxygen: Basic biochemical mechanisms. Amer. Zool.13, 543–555 (1973)Google Scholar
  21. Hohorst, H.: Substrates involved in the citric acid cycle. In: Methods in enzymatic analysis, Sect. II (H.U. Bergmeyer, ed.), pp. 328–334. New York: Academic Press 1965Google Scholar
  22. Holwerda, D.A., Zwaan, A. de: Kinetic and molecular characteristics of allosteric pyruvate kinase from muscle tissue of the sea musselMytilus edulis L. Biochem. biophys Acta (Amst.)309, 296–306 (1973)Google Scholar
  23. Klutmans, J.H.F.M., Veenhof, P.R., Zwaan, A. de: Anaerobic production of volatile fatty acids in the sea MusselMytilus edulis L. J. comp. Physiol.104, 71–78 (1975)Google Scholar
  24. Kmetec, E.: Spectrophotometric method for the enzymic microdetermination of succinic acid. Analyt. Biochem.16, 474–480 (1966)Google Scholar
  25. Lane, M.D., Chang, H.C., Miller, R.S.: Reactions Leading to and from the citric acid cycle. In: Methods in enzymology, Vol. XIII, Sect. II (S.P. Colowick, N.O. Kaplan, eds.), p. 270. New York: Academic Press 1969Google Scholar
  26. Livingstone, D.R.: Biochemical adaptations byMytilus edulis L. Ph. D. dissertation, University of Leicester, England (1975a)Google Scholar
  27. Livingstone, D.R.: A comparison of the kinetic properties of pyruvate kinase in three populations ofMytilus edulis L. from different environments. In: Proc 9th Europ. mar. biol. Symp. (H. Barnes, ed.), pp. 151–164. Aberdeen: Aberdeen University Press 1975bGoogle Scholar
  28. Livingstone, D.R., Bayne, B.L.: Pyruvate kinase from the mantle tissue ofMytilus edulis L. Comp. Biochem. Physiol.48B, 481–497 (1974)Google Scholar
  29. Loxton, J., Chaplin, A.E.: The metabolism ofMytilus edulis L. during facultative anaerobiosis. Biochem. Soc. Trans.2, 41–43 (1973)Google Scholar
  30. Matheson, A.T., Tattrie, B.L.: A modified Yemm and Cocking ninhydrin reagent for peptidase assay. Canad. J. Biochem.42, 95–103 (1964)Google Scholar
  31. Pfleiderer, G.: Substrates involved in protein metabolism. In: Methods in enzymatic analysis, Sect. III (H.U. Bergmeyer, ed.), pp. 378–380, New York: Academic Press 1965Google Scholar
  32. Prosser, C.L.: Comparative animal physiology. Philadelphia: W.B. Saunders Company 1973Google Scholar
  33. Schlieper, C.: Comparative study ofAsterias rubens andMytilus edulis from the North Sea (30‰S) and the Western Baltic Sea (15‰S). Annéc biol.33, 117–127 (1957)Google Scholar
  34. Simpson, J.W., Awapara, J.: The pathway of glucose degradation in some invertebrates. Comp. Biochem. Physiol.18, 537–548 (1966)Google Scholar
  35. Stokes, T., Awapara, J.: Alanine and succinate as end-products of glucose degradation in some invertebrates. Comp. Biochem. Physiol.25, 883–892 (1968)Google Scholar
  36. Storey, K.B., Hochachka, P.W.: Enzymes of energy metabolism in a vertebrate facultative anaerobe,Pseudemys scripta. Turtle heart pyruvate kinase. J. biol. Chem.249, 1423–1427 (1974a)Google Scholar
  37. Storey, K.B., Hochachka, P.W.: Glycolytic enzymes in muscle of the pacific dolphin: role of pyruvate kinase in aerobic-anaerobic transition during diving. Comp. Biochem. Physiol.49B, 119–128 (1974b)Google Scholar
  38. Trueman, E.R.: Activity and heart rate of bivalve molluscs in their natural habitat. Nature (Lond.)214, 832–833 (1967)Google Scholar
  39. Wegener, A., Barnitt, A.E., Hammen, C.S.: Reduction of fumarate and oxidation of succinate inCrassostrea virginica (Gmelin). Life Sci.8, 335–343 (1969)Google Scholar
  40. Zwaan, A. de: Pyruvate kinase in muscle extracts of the sea musselMytilus edulis L. Comp. Biochem. Physiol.42B, 7–14 (1972)Google Scholar
  41. Zwaan, A. de, Bont, A.M.T. de: Phosphoenolpyruvate carboxykinase from adductor muscle tissue of the sea musselMytilus edulis L. J. comp. Physiol.96, 85–94 (1975)Google Scholar
  42. Zwaan, A. de, Bont, A.M.T. de, Kluytmans, J.H.F.M.: Metabolic adaptations on the aerobicanaerobic transition in the sea musselMytilus edulis L. In: Proc. 9th Europ. mar. biol. Symp. (H. Barnes, ed.), pp. 121–138. Aberdeen: Aberdeen University Press 1975Google Scholar
  43. Zwaan, A. de, Holwerda, D.A.: The effect of phosphoenolpyruvate, fructose-1,6-diphosphate and pH on allosteric pyruvate kinase in muscle tissue of the bivalveMytilus edulis L. Biochim. biophys. Acta (Amst.)27b, 430–433 (1972)Google Scholar
  44. Zwaan, A. de, Klutymans, J.H.F.M., Zandee, D.I.: Facultative anaerobiosis in molluscs. Biochem. Soc. Symp.41, 133–168 (1976)Google Scholar
  45. Zwaan, A. de, Marrewijk, W.J.A. van: Anaerobic glucose degradation in the sea musselMytilus edulis L. Comp. Biochem. Physiol.44B, 429–439 (1973)Google Scholar
  46. Zwaan, A. de, Wijsman, T.C.M.: Anaerobic metabolism in Bivalvia (Mollusca)—I. Characteristics of anaerobic metabolism. Comp. Biochem. Physiol.54B, 313–324 (1976)Google Scholar
  47. Zwaan, A., de, Zandee, D.I.: The utilization of glycogen and accumulation of some intermediates during anaerobiosis inMytilus edulis L., Comp. Biochem. Physiol.43B, 47–54 (1972)Google Scholar

Copyright information

© Springer-Verlag 1977

Authors and Affiliations

  • D. R. Livingstone
    • 1
  • B. L. Bayne
    • 1
  1. 1.Institute for Marine Environmental ResearchPlymouthEngland

Personalised recommendations