Comparative studies on avian hemoglobins

doi:10.1016/0010-406X(65)90348-8

Comparative Biochemistry and Physiology

Volume 15, Issue 2, June 1965, Pages 217-235

https://doi.org/10.1016/0010-406X(65)90348-8 Get rights and content

Abstract

1.
1. Studies on paper electrophoretic mobility of hemoglobins obtained from avian species representing thirteen natural orders show that avian erythrocytes possess one, two or three hemoglobins.
2.
2. The avian hemoglobins may be categorized into five groups depending on the degree of mobility towards anode. Although the ratio of hemoglobin-1 to other hemoglobins varies considerably, hemoglobin-1 was found to be the major component.
3.
3. The avian hemoglobins are relatively resistant to alkaline denaturation and the resistance characteristics depend on individual species.
4.
4. Duck, chick, pigeon and dove show a comparable amino acid composition in hemoglobin-1 whereas a widely divergent amino acid composition has been found in hemoglobin-2 of duck and of chick.
5.
5. Wide differences in amino acid composition of α₂¹- and β₂¹-chains of duck, chick and pigeon have been observed.

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Comparative studies on chick hemoglobins
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K. Singer et al.
Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hemolytic disorders by means of alkali denaturation. II. Their identification by means of the method of fractional denaturation
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Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hemolytic disorders by means of alkali denaturation. II. Their identification by means of the method of fractional denaturation
Blood
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S. Wilson et al.
Separation of the valyl-leucyl and valyl-glutamyl polypeptide chains of horse globin by fractional precipitation and column chromatography
Canad. J. Biochem. Physiol.
(1959)
M.L. Anson et al.
Protein coagulation and its reversal; preparation of insoluble globin, soluble globin and heme
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(1930)
J.B. Chatterjea et al.
Electrophoretic analysis of hemoglobin in Cooley's anemia (Thalassemia). Evidences of interaction of Thalassemia gene with that of an abnormal hemoglobin
Bull. Calcutta Sch. Trop. Med.
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J.B. Chatterjea et al.
Hemoglobin E-Thalassemia disease
Indian J. Med. Sci.
(1957)
V. D'Amello et al.
Further studies on the embryonic chick hemoglobin. An electrophoretic and immunoelectrophoretic analysis
Acta Embryol. Morph. Exp.
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Multiple hemoglobins in birds
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Electrophoretic behavior of avian hemoglobins

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(1958)

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Electrophoretic characteristics and cell content of the hemoglobins of developing chick embryos

J. Exp. Zool.

(1964)

Cited by (16)

Gene duplication and the evolution of hemoglobin isoform differentiation in birds
2012, Journal of Biological Chemistry
Citation Excerpt :
A number of bird species are known to express three or four structurally distinct isoHbs in definitive erythrocytes (11, 14, 15, 74, 75), but in all such cases HbA and HbD (i.e. tetrameric assemblies that incorporate the products of αA- and αD-globin, respectively) represent the two main isoforms. HbD expression has also been secondarily lost in a number of avian taxa (e.g. pigeons, parakeets, cuckoos, jays, herons, storks, and penguins (74, 76–80)). The same appears to be true for crocodilians (30–32), the sister group to Aves.
The majority of bird species co-express two functionally distinct hemoglobin (Hb) isoforms in definitive erythrocytes as follows: HbA (the major adult Hb isoform, with α-chain subunits encoded by the α^A-globin gene) and HbD (the minor adult Hb isoform, with α-chain subunits encoded by the α^D-globin gene). The α^D-globin gene originated via tandem duplication of an embryonic α-like globin gene in the stem lineage of tetrapod vertebrates, which suggests the possibility that functional differentiation between the HbA and HbD isoforms may be attributable to a retained ancestral character state in HbD that harkens back to a primordial, embryonic function. To investigate this possibility, we conducted a combined analysis of protein biochemistry and sequence evolution to characterize the structural and functional basis of Hb isoform differentiation in birds. Functional experiments involving purified HbA and HbD isoforms from 11 different bird species revealed that HbD is characterized by a consistently higher O₂ affinity in the presence of allosteric effectors such as organic phosphates and Cl⁻ ions. In the case of both HbA and HbD, analyses of oxygenation properties under the two-state Monod-Wyman-Changeux allosteric model revealed that the pH dependence of Hb-O₂ affinity stems primarily from changes in the O₂ association constant of deoxy (T-state)-Hb. Ancestral sequence reconstructions revealed that the amino acid substitutions that distinguish the adult-expressed Hb isoforms are not attributable to the retention of an ancestral (pre-duplication) character state in the α^D-globin gene that is shared with the embryonic α-like globin gene.
Haematological changes associated with haemorrhage in the pigeon
1979, Comparative Biochemistry and Physiology -- Part A: Physiology
- 1.
  1. Haematological changes associated with haemorrhage in the pigeon have been investigated.
- 2.
  2. Haematocrit, haemoglobin, and plasma protein concentrations decreased immediately post-haemorrhage, fluctuated and returned to normal or were slightly elevated after 10 weeks. Plasma osmolality increased immediately post-haemorrhage, then decreased and returned to normal after 2 weeks. The MCHC value was significantly higher than the pre-haemorrhage value after 10 weeks.
- 3.
  3. Four haemoglobin bands were found on electrophoresis of normal pigeon blood. Marked changes in the percentage composition of the haemoglobin electrophoretogram were observed after haemorrhage and these returned to pre-haemorrhage values after 10 weeks.
- 4.
  4. The results are discussed in relation to the ability of pigeons to withstand haemorrhage.
The pH of body fluids from marine intertidal invertebrates
1977, Journal of Experimental Marine Biology and Ecology
The pH of the body fluids of 25 species of marine invertebrates from nine phyla was determined at temperatures to which these animals were acclimated. The gastrovascular fluid of several coelenterates and one species of flatworm was found to have pH values approximating to that of sea water. The coelomic fluid of nemertine, sipinculid, echiuroid, and annelid worms, as well as the heart fluid of several molluscs and the sternal sinus fluid of decapod crustaceans, were characterized by more alkaline pH values. Echinoderm polian vesicle fluid was characterized by slightly acidic pH values. The importance of the pH of the body to the respiratory physiology of marine invertebrates is discussed.
Translation of mammalian globin messenger RNAs in an avian reticulocyte cell-free system
1973, BBA Section Nucleic Acids And Protein Synthesis
A comparison of Maltese and Sicilian sparrow haemoglobins
1970, Comparative Biochemistry And Physiology
- 1.
  1. Maltese and Sicilian sparrows have very similar external features.
- 2.
  2. An electrophoretic examination showed that both groups of sparrows had two haemoglobins, I and II, and that the electrophoretic mobilities of the corresponding components were the same in the two groups. Small differences were found between the relative amounts of the haemoglobins I and II in the Maltese and Sicilian birds.
- 3.
  3. The tryptic peptide map of Maltese sparrow haemoglobin I was identical with that of Sicilian sparrow haemoglobin I, but was different from the map obtained from Maltese sparrow haemoglobin II which was identical with that from Sicilian sparrow haemoglobin II.
- 4.
  4. These results indicate a very close taxonomic relationship between Maltese and Sicilian sparrows.
Electrophoretic studies on hemoglobins of Brewer's blackbird Euphagus cyanocephalus
1970, Comparative Biochemistry And Physiology
- 1.
  1. Two populations of Brewer blackbirds were sampled for possible polymorphisms in hemoglobins. Unlike other proteins in this species (e.g. ovotransferrin) none was found, but the hemoglobins were present as a multiple molecular system.
- 2.
  2. Electrophoretic, chemical and spectral studies were performed to determine the nature of the multiple hemoglobin system. Structural analysis by comparison of monomers of the different tetramers indicated that avian hemoglobins are similar structurally to those of mammals.

View all citing articles on Scopus

^☆: Contribution No. 3155.

^†: Present address: McGill University, Royal Victoria Hospital, Montreal, Canada.

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Comparative Biochemistry and Physiology

Abstract

References (24)

The sulfhydryl groups of crystalline proteins I. Some albumins, enzymes and hemoglobins

J. Biol. Chem.

In vitro biosynthesis of chick hemoglobins

Biochim. Biophys. Res. Commun.

Comparative studies on chick hemoglobins

Biochim. Biophys. Acta

Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hemolytic disorders by means of alkali denaturation. II. Their identification by means of the method of fractional denaturation

Blood

Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hemolytic disorders by means of alkali denaturation. II. Their identification by means of the method of fractional denaturation

Blood

Separation of the valyl-leucyl and valyl-glutamyl polypeptide chains of horse globin by fractional precipitation and column chromatography

Canad. J. Biochem. Physiol.

Protein coagulation and its reversal; preparation of insoluble globin, soluble globin and heme

J. Gen. Physiol.

Electrophoretic analysis of hemoglobin in Cooley's anemia (Thalassemia). Evidences of interaction of Thalassemia gene with that of an abnormal hemoglobin

Bull. Calcutta Sch. Trop. Med.

Hemoglobin E-Thalassemia disease

Indian J. Med. Sci.

Further studies on the embryonic chick hemoglobin. An electrophoretic and immunoelectrophoretic analysis

Acta Embryol. Morph. Exp.

Multiple hemoglobins in birds

Experientia

Electrophoretic behavior of avian hemoglobins

Nature

Electrophoretic characteristics and cell content of the hemoglobins of developing chick embryos

J. Exp. Zool.

Cited by (16)

Gene duplication and the evolution of hemoglobin isoform differentiation in birds

Haematological changes associated with haemorrhage in the pigeon

The pH of body fluids from marine intertidal invertebrates

Translation of mammalian globin messenger RNAs in an avian reticulocyte cell-free system

A comparison of Maltese and Sicilian sparrow haemoglobins

Electrophoretic studies on hemoglobins of Brewer's blackbird Euphagus cyanocephalus

Comparative studies on avian hemoglobins☆

Abstract

J. Biol. Chem.

Biochim. Biophys. Res. Commun.

Biochim. Biophys. Acta

Blood

Blood

Canad. J. Biochem. Physiol.

Protein coagulation and its reversal; preparation of insoluble globin, soluble globin and heme

J. Gen. Physiol.

Electrophoretic analysis of hemoglobin in Cooley's anemia (Thalassemia). Evidences of interaction of Thalassemia gene with that of an abnormal hemoglobin

Bull. Calcutta Sch. Trop. Med.

Hemoglobin E-Thalassemia disease

Indian J. Med. Sci.

Further studies on the embryonic chick hemoglobin. An electrophoretic and immunoelectrophoretic analysis

Acta Embryol. Morph. Exp.

Multiple hemoglobins in birds

Experientia

Electrophoretic behavior of avian hemoglobins

Nature

Electrophoretic characteristics and cell content of the hemoglobins of developing chick embryos

J. Exp. Zool.