The ‘natural’ hybrid haemoglobin from mule. Interrelationships with its parent haemoglobins from horse and donkey.
Abstract: The equilibrium O2-binding properties of the hybrid haemoglobin (Hb) present in vivo in erythrocytes from mule and of its parent Hbs from horse and donkey were compared with special reference to the effect of heterotropic ligands such as Cl-, D-glycerate 2,3-bisphosphate (DPG) and inositol hexakisphosphate. All these Hbs display a decreased effect by polyphosphates, confirming that what has been observed for horse Hb [Giardina, Brix, Clementi, Scatena, Nicoletti, Cicchetti, Argentin & Condò (1990) Biochem. J. 266, 897-900] is common to other equine species, at least from a qualitative standpoint. However, different quantitative aspects can be detected, which can be accounted for by a different role for the two types of chain in characterizing the binding free energy for the various heterotropic effectors. In particular, it is shown that the binding mode of DPG and inositol hexakisphosphate displays different features since long-range effects can be observed clearly for inositol hexakisphosphate but not for DPG. In general terms, in spite of a different intrinsic O2 affinity, the modulation of functional properties by third ligands leads these Hbs to behave, under physiological conditions, similarly to human HbA. It might represent an interesting example of how different species with similar functional needs find different ways to produce a similar functional behaviour.
Publication Date: 1992-03-01 PubMed ID: 1546974PubMed Central: PMC1130823DOI: 10.1042/bj2820595Google Scholar: Lookup
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Summary
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The research examines the oxygen-binding properties of haemoglobin in mules and its parent species—horses and donkeys. Through the study, it was observed that, despite differences in oxygen affinity, various haemoglobins behave similarly under physiological conditions, possibly indicating how different species adapt to exhibit similar functionality.
Comparison of Haemoglobin Properties
- The researchers focused on the equilibrium oxygen-binding properties of the hybrid haemoglobin present in mules as well as its parent haemoglobins in horses and donkeys.
- They specifically looked at the effect of heterotropic ligands such as Cl-, D-glycerate 2,3-bisphosphate (DPG) and inositol hexakisphosphate on these haemoglobins.
- All these haemoglobins display a decreased effect by polyphosphates, which suggests a common line of properties across equine species.
Different Role of Chains in Characterizing Binding Free Energy
- But the researchers noted different quantitative aspects, which can be explained by differing roles for the two types of chains in determining the binding free energy for the various heterotropic effectors.
- The binding mode of DPG and inositol hexakisphosphate, two ligand substances, showcased varying characteristics—long-range effects were observed clearly for inositol hexakisphosphate while the same was not true for DPG.
Similarity of Haemoglobin Action Across Species
- In general terms, despite different natural affinities for oxygen, the modulation of haemoglobin’s functional properties by third ligands makes these haemoglobins behave similarly under physiological conditions.
- This could reflect a broader pattern in biology where different species that have similar functional needs may find diverse ways to produce similar functional behaviour, preserving their survival and viability in varied environments.
Cite This Article
APA
Condò SG, Coletta M, Cicchetti R, Argentin G, Guerrieri P, Marini S, el-Sherbini S, Giardina B.
(1992).
The ‘natural’ hybrid haemoglobin from mule. Interrelationships with its parent haemoglobins from horse and donkey.
Biochem J, 282 ( Pt 2)(Pt 2), 595-599.
https://doi.org/10.1042/bj2820595 Publication
Researcher Affiliations
- Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Italy.
MeSH Terms
- Animals
- Diphosphoglyceric Acids / metabolism
- Hemoglobins / metabolism
- Horses
- Isoelectric Point
- Perissodactyla / blood
- Phytic Acid / metabolism
- Species Specificity
References
This article includes 17 references
- Bailleul C, Borrelly-Villereal MC, Chassaigne M, Ropars C. Modification of partial pressure of oxygen (P50) in mammalian red blood cells by incorporation of an allosteric effector of hemoglobin.. Biotechnol Appl Biochem 1989 Feb;11(1):31-40.
- Giardina B, Brix O, Clementi ME, Scatena R, Nicoletti B, Cicchetti R, Argentin G, Condo SG. 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.
- Condò SG, Giardina B, Bellelli A, Brunori M. Xenopus laevis hemoglobin and its hybrids with hemoglobin A+.. Biochemistry 1987 Oct 20;26(21):6718-22.
- Bunn HF, Kitchen H. Hemoglobin function in the horse: the role of 2,3-diphosphoglycerate in modifying the oxygen affinity of maternal and fetal blood.. Blood 1973 Sep;42(3):471-9.
- Perutz MF. Species adaptation in a protein molecule.. Mol Biol Evol 1983 Dec;1(1):1-28.
- Perutz MF, Brunori M. Stereochemistry of cooperative effects in fish an amphibian haemoglobins.. Nature 1982 Sep 30;299(5882):421-6.
- Giardina B, Amiconi G. Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures.. Methods Enzymol 1981;76:417-27.
- Baldwin JM. The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.. J Mol Biol 1980 Jan 15;136(2):103-28.
- Perutz MF, Imai K. Regulation of oxygen affinity of mammalian haemoglobins.. J Mol Biol 1980 Jan 15;136(2):183-91.
- Nigen AM, Manning JM, Alben JO. Oxygen-linked binding sites for inorganic anions to hemoglobin.. J Biol Chem 1980 Jun 25;255(12):5525-9.
- Imai K, Ikeda-Saito M, Yamamoto H, Yonetani T. Studies on cobalt myoglobins and hemoglobins X. Determination of microscopic oxygen-equilibrium constants of iron--cobalt hybrid hemoglobins and their parent hemoglobins.. J Mol Biol 1980 Apr 15;138(3):635-48.
- FANELLI AR, ANTONINI E, CAPUTO A. Studies on the structure of hemoglobin. I. Physicochemical properties of human globin.. Biochim Biophys Acta 1958 Dec;30(3):608-15.
- MONOD J, WYMAN J, CHANGEUX JP. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.. J Mol Biol 1965 May;12:88-118.
- O'Donnell S, Mandaro R, Schuster TM, Arnone A. X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1 alpha.. J Biol Chem 1979 Dec 10;254(23):12204-8.
- Nagai K. The effect of ferric ligands on the oxygen affinity of the ferrous subunits in valency hybrid haemoglobins.. J Mol Biol 1977 Mar 25;111(1):41-53.
- Giardina B, Brix O, Colosimo A, Petruzzelli R, Cerroni L, Condo SG. Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach.. Eur J Biochem 1990 Nov 26;194(1):61-5.
- 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.
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