Journal of Comparative Physiology B

, Volume 159, Issue 2, pp 205–209 | Cite as

Comparative oxygen affinity of fish and mammalian myoglobins

  • J. W. Nichols
  • L. J. Weber


Myoglobins from rat, coho salmon (Oncorhynchus kisutch), buffalo sculpin (Enophrys bison) hearts, and yellowfin tuna (Thunnus albacares) red skeletal muscle were partially purified and their O2 binding affinities determined. Commercially prepared sperm whale myoglobin was employed as an internal standard. Tested at 20°C, myoglobins from salmon and sculpin bound O2 with lower affinity than myoglobins from the rat or sperm whale. Oxygen binding studies at 12°C and 37°C suggest that this difference is adaptive, permitting myoglobins from cold-adapted fish to function at physiologically relevant temperatures. Taken together, purification and O2 binding data obtained in this study reveal a previously unrecognized diversity of myoglobin structure and function.

Key words

Fish Myoglobin Oxygen binding affinity 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Antonini E, Brunori M (1971) Hemoglobin and myoglobin in their reactions with ligands. In: Neuberger A, Tatum EL (eds) Frontiers of biology, vol 21. American Elsevier, New YorkGoogle Scholar
  2. Bailey JR, Driedzic WR (1986) Function of myoglobin in oxygen consumption by isolated perfused fish hearts. Am J Physiol 251:R1144-R1150Google Scholar
  3. Braunlin EA, Wahler GM, Swayze CR, Lucas RV, Fox IJ (1986) Myoglobin facilitated oxygen diffusion maintains mechanical function of mammalian cardiac muscle. Cardiovasc Res 20:627–634Google Scholar
  4. Carey FG, Teal JM, Kanwisher JF, Lawson KD, Beckett JS (1972) Warm-bodied fish. Am Zool 11:135–143Google Scholar
  5. Choromanski JM (1985) Chemical stabilization and pharmacological characterization of the venom of the lionfish (Pterois volitans). MS thesis, Oregon State University, Corvallis, OregonGoogle Scholar
  6. Cole RP (1982) Myoglobin function in exercising skeletal muscle. Science 216:523–525Google Scholar
  7. Colonna G, Irace G, Bismuto E, Servillo L, Balestrieri C (1983) Stuctural and functional aspects of the heart ventricle myoglobin of bluefin tuna. Comp Biochem Physiol 76 (A):481–485Google Scholar
  8. Covell DG, Jacquez JA (1987) Does myoglobin contribute significantly to diffusion of oxygen in red skeletal muscle? Am J Physiol 252:R341-R347Google Scholar
  9. Douglas EL, Peterson KS, Gysi JR, Chapman DJ (1985) Myoglobin in the heart tissue of fishes lacking hemoglobin. Comp Biochem Physiol 81A:885–888Google Scholar
  10. Driedzic WR (1983) The fish heart as a model system for the study of myoglobin. Comp Biochem Physiol 76A:487–493Google Scholar
  11. Driedzic WR, Stewart JM (1982) Myoglobin content and the activities of enzymes of energy metabolism in red and white fish hearts. J Comp Physiol 149:67–73Google Scholar
  12. Driedzic WR, Stewart JM, Scott DL (1982) The protective effect of myoglobin during hypoxic perfusion of isolated fish hearts. J Mol Cell Cardiol 14:673–677Google Scholar
  13. Federspiel WJ (1986) A model study of intracellular oxygen gradients in a myoglobin-containing skeletal muscle fiber. Biophys J 49:857–868Google Scholar
  14. Fosmire GJ, Brown WD (1976) Yellowfin tuna (Thunnus albacares) myoglobin: characterization and comparative stability. Comp Biochem Physiol 55B:293–299Google Scholar
  15. Giovane A, Maresca GA, Tota B (1980) Myoglobin in the heart ventricle of tuna and other fishes. Experientia 36:219–220Google Scholar
  16. Hayashi A, Suzuki T, Shin M (1973) An enzymatic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Biochim Biophys Acta 310:309–316Google Scholar
  17. Lattman EE, Nockolds CE, Kretsinger RH, Love WE (1971) Stucture of yellowfin tuna metmyoglobin at 6A resolution. J Mol Biol 60:271–277Google Scholar
  18. Millikan GA (1939) Muscle hemoglobin. Physiol Rev 19:503–523Google Scholar
  19. Riggs A (1951) The metamorphosis of hemoglobin in the bullfrog. J Gen Physiol 35:23–40Google Scholar
  20. Rossi Fanelli A, Antonini E, Giuffre R (1960) Oxygen equilibrium ofThunnus thynnus. Nature 186:896–897Google Scholar
  21. Taylor DJ, Matthews PM, Radda GK (1986) Myoglobin-dependent oxidative metabolism in the hypoxic rat heart. Resp Physiol 63:275–283Google Scholar
  22. Watts DA, Rice RH, Brown DB (1980) The primary structure of myoglobin from yellowfin tuna (Thunnus albacares). J Biol Chem 255:10916–10924Google Scholar
  23. Wittenberg JB (1970) Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol Rev 50:559–636Google Scholar
  24. Wittenberg JB, Wittenberg BA (1981) Preparation of myoglobins. In: Antonini E, Rossi-Bernardi L, Chiancone E (eds) Methods in enzymology, vol 76: Hemoglobins. Academic Press, New YorkGoogle Scholar
  25. Wittenberg BA, Wittenberg JB, Calawell PRB (1975) Role of myoglobin in the oxygen supply to red skeletal muscle. J Biol Chem 250:9038–9043Google Scholar
  26. Yamazaki I, Yokota K, Shikama K (1964) Preparation of crystalline oxymyoglobin from horse heart. J Biol Chem 239:4151–4153Google Scholar

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • J. W. Nichols
    • 1
  • L. J. Weber
    • 1
  1. 1.Hatfield Marine Science CenterOregon State UniversityNewportUSA

Personalised recommendations