Evolution of ruminant hemoglobins

Giardina, Bruno; Arévalo, F.; Clementi, Maria Elisabetta; Ferrara, Lucio; Luccia, Aldo Di; Lendaro, Eugenio; Bellelli, Andrea; Condò, Saverio G.

doi:10.1111/j.1432-1033.1992.tb16661.x

Cited by 10 publications

(5 citation statements)

References 19 publications

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“…The amplitude of the Bohr effect (Siog P50/8pH; where 8pH = 6.0-8.0) for 02 binding to chamois and steinbock Hb in the presence of 0.1 M NaCl (0.43) is the same as that observed for oxygenation of human Hb, which is higher than that observed for other ruminant Hbs (Fronticelli et al, 1988;Giardina et al, 1990aGiardina et al, , 1992adi Prisco et al, 1991). In fact, the amplitude of the Bohr effect for 02 binding to reindeer Hb (0.28) is about 35 % less than that of human, chamois and steinbock Hb, in the 408 nm) and 187 mM'cm-' (at 407 nm) respectively at pH 6.5 absence, of Gri(2,3)P,.…”

Section: Resultsmentioning

confidence: 60%

“…reindeer, musk ox, red deer and ox) are lower, ranging between approx. -10 and -15 kJ/mol [Giardina et al (1992a) and Coletta et al (1992)]. Table 1 gives values of the overall first-order rate constants for 02 dissociation from ligated human, reindeer, chamois and steinbock Hb (i.e., values of koff), in the absence and presence of allosteric effectors at pH 7.4 and 20 'C.…”

Section: Resultsmentioning

confidence: 99%

“…Oxygenated Hb samples from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex) were prepared as follows (Antonini and Brunori, 1971;Giardina et al, 1990aGiardina et al, , 1992a. Fresh blood samples from these two animals were obtained from Centro Studi di Fauna Alpina, Parco Nazionale del Gran Paradiso, Noasca (TO), Italy.…”

Section: Methodsmentioning

confidence: 99%

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Functional, spectroscopic and structural properties of haemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex)

Ascenzi

Clementi

Condò

et al. 1993

Biochemical Journal

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The functional and spectroscopic properties of chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex) haemoglobin (Hb) have been studied with special reference to the action of allosteric effectors and temperature. Moreover, the amino acid sequences of the N-terminal segments of the alpha- and beta-chains have been determined. The present results indicate that chamois and steinbock Hbs display a low affinity for O2, which appears to be modulated in vivo by Cl- ions rather than 2,3-bisphosphoglycerate. The Bohr effect for O2 binding to chamois and steinbock Hb is higher than for reindeer and bovine Hbs, being similar to that of human Hb. Moreover, the temperature-dependence of oxygenation appears intermediate between that of human and reindeer Hbs. E.p.r. and absorption spectroscopic properties of the ferrous nitrosylated derivative of chamois and steinbock Hbs suggest that both haemoproteins are in a low-affinity conformation even in the absence of InsP6. The reduced effect of polyphosphates on the functional and spectroscopic properties of chamois and steinbock Hb agree with amino acid differences in the N-terminal segment of the beta-chains (i.e. the deletion of Val(NA1) and the replacement of His(NA2), present in human Hb, and Gln(NA2), present in horse Hb, by Met). The molecular mechanism modulating the basic reaction of O2 with chamois and steinbock Hb may be linked to specific physiological needs related to the high-altitude habitats of these two animals.

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Section: Resultsmentioning

confidence: 60%

Section: Resultsmentioning

confidence: 99%

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Functional, spectroscopic and structural properties of haemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex)

Ascenzi

Clementi

Condò

et al. 1993

Biochemical Journal

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“…The work done over the years on haemoglobins from different species has pointed out the physiological importance of the overall enthalpy change associated with the reaction of Hb with oxygen [1][2][3][4]. In fact, binding of oxygen to Hb is generally an exothermic reaction and a decrease in temperature induces an increase in oxygen affinity.…”

Section: Introductionmentioning

confidence: 99%

From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin

Rosa

Castagnola

Bertonati

et al. 2004

Biochemical Journal

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Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower Delta H of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as cow, horse and pig). This has been interpreted as an adaptive mechanism of great importance from a physiological point of view. To date, the molecular basis of this thermodynamic characteristic is still not known. In the present study, we show that binding of extra chloride (with respect to adult human Hb) ions to Hb would significantly contribute to lowering the overall heat of oxygenation, thus providing a molecular basis for the low effect of temperature on the oxygenation-deoxygenation cycle. To this aim, the oxygen binding properties of bovine Hb, bear (Ursus arctos) Hb and horse Hb, which are representative of this series of haemoglobins, have been studied with special regard to the effect of heterotropic ligands, such as organic phosphates (namely 2,3-diphosphoglycerate) and chloride. Functional results are consistent with a mechanism for ligand binding that involves an additional binding site for chloride ion. Analysis of computational chemistry results, obtained by the GRID program, further confirm the hypothesis that the reason for the lower Delta H of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites.

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“…The biochemical polymorphism of hemoglobin in the water buffalo has been previously described, both by investigating the possible adaptive significance of buffalo hemoglobin structure and thermodynamic properties (Giardina et al, 1992) and by analysing the variation in the alpha globin system and beta globin locus (Di Luccia et al, 1989;Di Luccia et al, 1991a;Di Luccia et al, 1991b).…”

Section: Introductionmentioning

confidence: 99%

Biochemical and molecular investigations on qualitative and quantitative Hb polymorphism in the river buffalo (Bubalus bubalis L.) population reared in Southern Italy

Iorio¹,

Vincenti²,

Annunziata³

et al. 2004

Genet. Mol. Biol.

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On 398 river buffalo samples, randomly collected in distinct breeding areas of the Campania region, high-resolution analytical systems were used to identify both qualitative and quantitative variations of the Hb phenotype. Polyacrylamide gel isoelectric focusing and HPLC were used to determine the ratio between HBA1 and HBA2 globin chains; restriction endonuclease analysis was performed to assess whether quantitative variations in Hb bands were related to an unusual number of α-globin genes. In the two buffalo subpopulations, allele frequencies of the alpha and beta globin systems were calculated, and F statistics (FIS, FIT and FST) were estimated as parameters of genetic diversity. The results suggest that: i) as shown by RFLP analysis, only a couple of associated α globin genes account for the quantitative variations recorded at the phenotypic level; ii) as expected, in the α globin gene system (HBA), the frequency of haplotype B (HBA-B) largely exceeded that of haplotype A (HBA-A) (95.1% vs 4.9%); iii) the frequency of the usual allele at the beta locus is 0.6, as opposed to 0.4 of the slow variant; iiii) the most significant component of variation of the genetic system of hemoglobin is between individuals within the same location.

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Evolution of ruminant hemoglobins

Cited by 10 publications

References 19 publications

Functional, spectroscopic and structural properties of haemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex)

Functional, spectroscopic and structural properties of haemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex)

From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin

Biochemical and molecular investigations on qualitative and quantitative Hb polymorphism in the river buffalo (Bubalus bubalis L.) population reared in Southern Italy

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