Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Oct 15;271(2):509–513. doi: 10.1042/bj2710509

Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata).

O Brix 1, S G Condò 1, A Bardgard 1, B Tavazzi 1, B Giardina 1
PMCID: PMC1149584  PMID: 2122890

Abstract

The functional properties of haemoglobin from the Lesser Rorqual whale (Balaenoptera acutorostrata) have been characterized as a function of the heterotropic effector concentrations and temperature. The results obtained suggest the existence of sophisticated modulation mechanisms based on the interplay of organic phosphates, carbon dioxide, lactate and temperature. These, together with the very small apparent heat of oxygenation (delta H) of oxygen binding, have been physiologically interpreted on the basis of the specific metabolic needs of this diving mammal.

Full text

PDF
511

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amiconi G., Antonini E., Brunori M., Wyman J., Zolla L. Interaction of hemoglobin with salts. Effects on the functional properties of human hemoglobin. J Mol Biol. 1981 Oct 15;152(1):111–129. doi: 10.1016/0022-2836(81)90097-8. [DOI] [PubMed] [Google Scholar]
  2. Baldwin J. M. The structure of human carbonmonoxy haemoglobin at 2.7 A resolution. J Mol Biol. 1980 Jan 15;136(2):103–128. doi: 10.1016/0022-2836(80)90308-3. [DOI] [PubMed] [Google Scholar]
  3. Benesch R. E., Benesch R., Yu C. I. The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. Biochemistry. 1969 Jun;8(6):2567–2571. doi: 10.1021/bi00834a046. [DOI] [PubMed] [Google Scholar]
  4. Condò S. G., Giardina B., Bellelli A., Brunori M. Xenopus laevis hemoglobin and its hybrids with hemoglobin A+. Biochemistry. 1987 Oct 20;26(21):6718–6722. doi: 10.1021/bi00395a022. [DOI] [PubMed] [Google Scholar]
  5. Condó S. G., el-Sherbini S., Shehata Y. M., Serpe E., Nuutinen M., Lazzarino G., Giardina B. Regulation of the oxygen affinity of haemoglobin from the reindeer (Rangifer tarandus tarandus L.). Arctic Med Res. 1988 Apr;47(2):83–88. [PubMed] [Google Scholar]
  6. Dhindsa D. S., Metcalfe J., Hoversland A. S., Hartman R. A. Comparative studies of the respiratory functions of mammalian blood. X. Killer whale (Orcinus orca linnaeus) and beluga whale (Delphin apterus leucas). Respir Physiol. 1974 Mar;20(2):93–103. doi: 10.1016/0034-5687(74)90099-1. [DOI] [PubMed] [Google Scholar]
  7. Giardina B., Amiconi G. Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures. Methods Enzymol. 1981;76:417–427. doi: 10.1016/0076-6879(81)76133-0. [DOI] [PubMed] [Google Scholar]
  8. Giardina B., Brix O., Clementi M. E., Scatena R., Nicoletti B., Cicchetti R., Argentin G., Condo S. G. Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding. Biochem J. 1990 Mar 15;266(3):897–900. [PMC free article] [PubMed] [Google Scholar]
  9. Giardina B., Brix O., Nuutinen M., el Sherbini S., Bardgard A., Lazzarino G., Condò S. G. Arctic adaptation in reindeer. The energy saving of a hemoglobin. FEBS Lett. 1989 Apr 10;247(1):135–138. doi: 10.1016/0014-5793(89)81256-6. [DOI] [PubMed] [Google Scholar]
  10. Guesnon P., Poyart C., Bursaux E., Bohn B. The binding of lactate and chloride ions to human adult hemoglobin. Respir Physiol. 1979 Oct;38(2):115–129. doi: 10.1016/0034-5687(79)90031-8. [DOI] [PubMed] [Google Scholar]
  11. Jelkmann W., Oberthür W., Kleinschmidt T., Braunitzer G. Adaptation of hemoglobin function to subterranean life in the mole, Talpa europaea. Respir Physiol. 1981 Oct;46(1):7–16. doi: 10.1016/0034-5687(81)90064-5. [DOI] [PubMed] [Google Scholar]
  12. Kilmartin J. V., Rossi-Bernardi L. Interaction of hemoglobin with hydrogen ions, carbon dioxide, and organic phosphates. Physiol Rev. 1973 Oct;53(4):836–890. doi: 10.1152/physrev.1973.53.4.836. [DOI] [PubMed] [Google Scholar]
  13. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  14. Perutz M. F., Imai K. Regulation of oxygen affinity of mammalian haemoglobins. J Mol Biol. 1980 Jan 15;136(2):183–191. doi: 10.1016/0022-2836(80)90312-5. [DOI] [PubMed] [Google Scholar]
  15. Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature. 1970 Nov 21;228(5273):726–739. doi: 10.1038/228726a0. [DOI] [PubMed] [Google Scholar]
  16. Reeves R. B. The effect of temperature on the oxygen equilibrium curve of human blood. Respir Physiol. 1980 Dec;42(3):317–328. doi: 10.1016/0034-5687(80)90122-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES