FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
The Biochemical journal1990; 266(3); 897-900;

Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding.

Abstract: Despite the fact that the horse is one of the more common domesticated animals, there are few reports dealing with the properties of its blood, and no comprehensive study has been performed on the reactivity of horse haemoglobin towards organic and inorganic ions. Here we report data on the effects of the organic phosphates D-glycerate-2,3-bisphosphate (2,3-DPG) and InsP6, and of chloride on the properties of horse haemoglobin. Thus the effect of saturating concentrations of 2,3-DPG on the oxygen affinity of horse haemoglobin is about 60% lower than with human adult haemoglobin under the same experimental conditions. The same applies also to InsP6, whose effect on oxygen binding to horse haemoglobin is decreased by about 55% compared with human adult haemoglobin. On the whole, horse haemoglobin appears to be much less sensitive to organic phosphates than previously believed. These results are discussed in the light of the primary structure of the molecule.
Get Full Text
Publication Date: 1990-03-15 PubMed ID: 2327974PubMed Central: PMC1131223
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Comparative Study
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigates the effects of certain organic and inorganic ions on the properties of horse haemoglobin, revealing distinct differences compared to human haemoglobin in response to these ions.

Objective of the Study

The main objective of this study was to conduct a comprehensive investigation into the effects of specific organic and inorganic ions on horse haemoglobin. The study sought to discover how these effects compare with those on human haemoglobin, as previous studies on this topic are limited.

Methods and Materials

  • The ions tested on the horse haemoglobin were organic phosphates D-glycerate-2,3-bisphosphate (2,3-DPG), InsP6, and an inorganic ion – chloride.
  • The researchers used saturating concentrations of these ions to study their effect on the oxygen affinity of horse haemoglobin.
  • These results were then compared against the effects observed under the same conditions on human adult haemoglobin.

Results and Findings

  • The researchers found that the effect of saturating concentrations of 2,3-DPG on the oxygen affinity of horse haemoglobin is approximately 60% lower than on human adult haemoglobin.
  • InsP6, another organic phosphate, also showed a reduced effect on oxygen binding to horse haemoglobin by about 55% compared with human haemoglobin.
  • Overall, the study concluded that horse haemoglobin exhibits a much lower sensitivity to organic phosphates than what was previously understood.

Implications

These findings are important because they lay the groundwork for a more in-depth understanding of the biological behavior of horse haemoglobin and its interaction with specific ions. This difference in sensitivity between horse and human haemoglobin to organic phosphates could have broader biological and clinical implications, especially in veterinary medicine and potentially in developing animal models for human diseases. The researchers plan on continuing this line of investigation in light of the primary structure of the molecule.

Cite This Article

APA
Giardina B, Brix O, Clementi ME, Scatena R, Nicoletti B, Cicchetti R, Argentin G, Condo SG. (1990). Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding. Biochem J, 266(3), 897-900.

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 266
Issue: 3
Pages: 897-900

Researcher Affiliations

Giardina, B
  • Department of Experimental Medicine and Biochemical Sciences, University of Rome, Italy.
Brix, O
    Clementi, M E
      Scatena, R
        Nicoletti, B
          Cicchetti, R
            Argentin, G
              Condo, S G

                MeSH Terms

                • 2,3-Diphosphoglycerate
                • Amino Acid Sequence
                • Animals
                • Chlorides / pharmacology
                • Diphosphoglyceric Acids / pharmacology
                • Hemoglobins / metabolism
                • Horses / blood
                • Humans
                • Molecular Sequence Data
                • Oxygen / metabolism

                References

                This article includes 23 references
                1. Arnone A. X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin.. Nature 1972 May 19;237(5351):146-9.
                  pubmed: 4555506doi: 10.1038/237146a0google scholar: lookup
                2. Yousef MK, Burk D, Dill DB. Biochemical properties of the blood of three equines.. Comp Biochem Physiol B 1971 Jun 15;39(2):279-84.
                  pubmed: 5119904doi: 10.1016/0305-0491(71)90170-2google scholar: lookup
                3. McLean JG, Lewis IM. Oxygen affinity responses to 2,3-diphosphoglycerate, and methaemoglobin formation in horse and human haemoglobins.. Res Vet Sci 1975 Nov;19(3):259-62.
                  pubmed: 1215675
                4. Frier JA, Perutz MF. Structure of human foetal deoxyhaemoglobin.. J Mol Biol 1977 May 5;112(1):97-112.
                  pubmed: 881729doi: 10.1016/s0022-2836(77)80158-7google scholar: lookup
                5. Braunitzer G, Schrank B, Stangl A, Bauer C. [Regulation of respiration at high altitudes and its molecular interpretation: the sequence of beta-chains of hemoglobins from pig and llama (author's transl)].. Hoppe Seylers Z Physiol Chem 1977 Jul;358(7):921-5.
                  pubmed: 892715
                6. Perutz MF, Imai K. Regulation of oxygen affinity of mammalian haemoglobins.. J Mol Biol 1980 Jan 15;136(2):183-91.
                  pubmed: 7373649doi: 10.1016/0022-2836(80)90312-5google scholar: lookup
                7. Matsuda G, Maita T, Braunitzer G, Schrank B. [Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author's transl)].. Hoppe Seylers Z Physiol Chem 1980 Jul;361(7):1107-16.
                  pubmed: 7409745
                8. Bunn HF. Evolution of mammalian hemoglobin function.. Blood 1981 Aug;58(2):189-97.
                  pubmed: 7018619
                9. Giardina B, Amiconi G. Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures.. Methods Enzymol 1981;76:417-27.
                  pubmed: 7329266doi: 10.1016/0076-6879(81)76133-0google scholar: lookup
                10. 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.
                  pubmed: 7330493doi: 10.1016/0034-5687(81)90064-5google scholar: lookup
                11. 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):111-29.
                  pubmed: 7338905doi: 10.1016/0022-2836(81)90097-8google scholar: lookup
                12. Clegg JB, Goodbourn SE, Braend M. Genetic organization of the polymorphic equine alpha globin locus and sequence of the BII alpha 1 gene.. Nucleic Acids Res 1984 Oct 25;12(20):7847-58.
                  pubmed: 6093055doi: 10.1093/nar/12.20.7847google scholar: lookup
                13. Bucci E, Fronticelli C. Anion Bohr effect of human hemoglobin.. Biochemistry 1985 Jan 15;24(2):371-6.
                  pubmed: 3978079doi: 10.1021/bi00323a020google scholar: lookup
                14. Kleinschmidt T, Sgouros JG. Hemoglobin sequences.. Biol Chem Hoppe Seyler 1987 Jun;368(6):579-615.
                  pubmed: 3304337
                15. Perutz MF. Species adaptation in a protein molecule.. Mol Biol Evol 1983 Dec;1(1):1-28.
                  pubmed: 6400645doi: 10.1093/oxfordjournals.molbev.a040299google scholar: lookup
                16. Condó SG, el-Sherbini S, Shehata YM, 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):83-8.
                  pubmed: 3166648
                17. Fronticelli C, Bucci E, Razynska A. Modulation of oxygen affinity in hemoglobin by solvent components. Interaction of bovine hemoglobin with 2,3-diphosphoglycerate and monatomic anions.. J Mol Biol 1988 Jul 20;202(2):343-48.
                  pubmed: 2845098doi: 10.1016/0022-2836(88)90463-9google scholar: lookup
                18. Giardina B, Brix O, Nuutinen M, el Sherbini S, Bardgard A, Lazzarino G, Condò SG. Arctic adaptation in reindeer. The energy saving of a hemoglobin.. FEBS Lett 1989 Apr 10;247(1):135-8.
                  pubmed: 2707444doi: 10.1016/0014-5793(89)81256-6google scholar: lookup
                19. Benesch R, Benesch RE. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin.. Biochem Biophys Res Commun 1967 Jan 23;26(2):162-7.
                  pubmed: 6030262doi: 10.1016/0006-291x(67)90228-8google scholar: lookup
                20. Chanutin A, Curnish RR. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes.. Arch Biochem Biophys 1967 Jul;121(1):96-102.
                  pubmed: 6035074doi: 10.1016/0003-9861(67)90013-6google scholar: lookup
                21. Miwa I, Erdös EG, Seki T. Presence of three peptides in urinary kinin (substance Z) preparations.. Life Sci 1968 Dec 15;7(24):1339-43.
                  pubmed: 5711936doi: 10.1016/0024-3205(68)90265-8google scholar: lookup
                22. Bunn HF. Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins.. Science 1971 Jun 4;172(3987):1049-50.
                  pubmed: 5573955doi: 10.1126/science.172.3987.1049google scholar: lookup
                23. Chiancone E, Norne JE, Forsén S, Bonaventura J, Brunori M, Antonini E, Wyman J. Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests.. Eur J Biochem 1975 Jul 1;55(2):385-90.
                  pubmed: 236doi: 10.1111/j.1432-1033.1975.tb02173.xgoogle scholar: lookup

                Citations

                This article has been cited 7 times.
                1. Gevorkian SG, Allahverdyan AE, Gevorgyan DS, Hu CK. Thermal-induced force release in oxyhemoglobin. Sci Rep 2015 Aug 17;5:13064.
                  doi: 10.1038/srep13064pubmed: 26277901google scholar: lookup
                2. Soares JH, Brosnan RJ, Fukushima FB, Hodges J, Liu H. Solubility of haloether anesthetics in human and animal blood. Anesthesiology 2012 Jul;117(1):48-55.
                  doi: 10.1097/ALN.0b013e3182557cc9pubmed: 22510863google scholar: lookup
                3. Manconi B, Messana I, Maggiani F, Olianas A, Pellegrini M, Crnjar R, Castagnola M, Giardina B, Sanna MT. Structural and functional characterization of Delphinus delphis hemoglobin system. J Comp Physiol B 2009 Nov;179(8):971-83.
                  doi: 10.1007/s00360-009-0380-2pubmed: 19554331google scholar: lookup
                4. Remington N, Stevens RD, Wells RS, Holn A, Dhungana S, Taboy CH, Crumbliss AL, Henkens R, Bonaventura C. Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins. Gene 2007 Aug 15;398(1-2):123-31.
                  doi: 10.1016/j.gene.2007.02.050pubmed: 17604574google scholar: lookup
                5. Brix O, Condò SG, Bardgard A, Tavazzi B, Giardina B. Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata). Biochem J 1990 Oct 15;271(2):509-13.
                  doi: 10.1042/bj2710509pubmed: 2122890google scholar: lookup
                6. Condò SG, Coletta M, Cicchetti R, Argentin G, Guerrieri P, Marini S, el-Sherbini S, Giardina B. The 'natural' hybrid haemoglobin from mule. Interrelationships with its parent haemoglobins from horse and donkey. Biochem J 1992 Mar 1;282 ( Pt 2)(Pt 2):595-9.
                  doi: 10.1042/bj2820595pubmed: 1546974google scholar: lookup
                7. Shibayama N. Effects of allosteric effectors on oxygen binding to crystals of hemoglobin in the R-quaternary structure. Protein Sci 2025 Jan;34(1):e5232.
                  doi: 10.1002/pro.5232pubmed: 39660833google scholar: lookup
                Subscribe to our newsletter
                Join 99,780 horse owners like you who receive our email updates on horse health and nutrition.