Amino-Acid Sequence of the α<sup>D</sup>- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin

We determined the complete amino acid sequences of the hemoglobin of two species, guinea fowl and California quail, in Galliformes from intact globin chain and chemical cleavage fragments in order to analyze the molecular evolution of hemoglobin for the classification of Galliformes. Galliformes have two types of hemoglobin components, HbA and HbD, which consist of identical beta chain and different alpha chains. The sequences are similar to globin chains of Galliformes reported previously. These sequences were compared with those of other Galliformes (Phasianidae, Meleagrididae) using duck and goshawk as out-groups. The phylogenetic tree of major groups of Galliformes based on hemoglobin was similar to the tree model produced based on the amino acid sequence of lysozyme c.

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Amino Acid Sequences of Hemoglobin from Guinea Fowl (Numida meleagri) and California Quail (Lophortyx californica) with Phylogenetic Analysis of Major Groups of Galliformes

Eguchi

Ikehara

Eguchi

2000

J Protein Chem

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Alkaline Bohr effect of bird hemoglobins: the case of the flamingo

Sanna¹,

Manconi²,

Podda³

et al. 2007

BCHM

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The hemoglobin (Hb) substitution His-->Gln at position alpha89, very common in avian Hbs, is considered to be responsible for the weak Bohr effect of avian Hbs. Phoenicopterus ruber ruber is one of the few avian Hbs that possesses His at alpha89, but it has not been functionally characterized yet. In the present study the Hb system of the greater flamingo (P. ruber roseus), a bird that lives in Mediterranean areas, has been investigated to obtain further insight into the role played by the alpha89 residue in determining the strong reduction of the Bohr effect. Functional analysis of the two purified Hb components (HbA and HbD) of P. ruber roseus showed that both are characterized by high oxygen affinity in the absence of organic phosphates, a strong modulating effect of inositol hexaphosphate, and a reduced Bohr effect. Indeed, in spite of the close phylogenetic relationship between the two flamingo species, structural analysis based on tandem mass spectrometry of the alpha(A) chain of P. ruber roseus Hb showed that a Gln residue is present at position alpha89.

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Short Communication

Eguchi

Takei²

1994

Biological Chemistry Hoppe-Seyler

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Only one hemoglobin component is recognized in the erythrocytes of the adult Ryukyu rufous turtle dove. We have determined the amino acid sequence of the alpha A-globin and the beta-globin by conventional protein sequence analysis. The sequences of both the alpha A- and the beta-globins were highly similar to domestic pigeon hemoglobin. The alpha A-globin has 6 exchanges and beta-globin has 4 exchanges compared with the corresponding domestic pigeon chains.

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Amino-Acid Sequence of the α^D- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin

Abstract: 4) Amino-acid sequence analysisAn automated amino-acid sequence analysis was carried out using a gas phase automatic sequence analyzer (Model PSQ-1, Shimadzu Co., Kyoto) equipped with an online PTH analyzer (Model, PTH-1, Shimadzu Co.).

Cited by 4 publications

References 10 publications

Amino Acid Sequences of Hemoglobin from Guinea Fowl (Numida meleagri) and California Quail (Lophortyx californica) with Phylogenetic Analysis of Major Groups of Galliformes

Amino Acid Sequences of Hemoglobin from Guinea Fowl (Numida meleagri) and California Quail (Lophortyx californica) with Phylogenetic Analysis of Major Groups of Galliformes

Alkaline Bohr effect of bird hemoglobins: the case of the flamingo

Short Communication

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Amino-Acid Sequence of the αD- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin

Abstract: 4) Amino-acid sequence analysisAn automated amino-acid sequence analysis was carried out using a gas phase automatic sequence analyzer (Model PSQ-1, Shimadzu Co., Kyoto) equipped with an online PTH analyzer (Model, PTH-1, Shimadzu Co.).

Cited by 4 publications

References 10 publications

Amino Acid Sequences of Hemoglobin from Guinea Fowl (Numida meleagri) and California Quail (Lophortyx californica) with Phylogenetic Analysis of Major Groups of Galliformes

Amino Acid Sequences of Hemoglobin from Guinea Fowl (Numida meleagri) and California Quail (Lophortyx californica) with Phylogenetic Analysis of Major Groups of Galliformes

Alkaline Bohr effect of bird hemoglobins: the case of the flamingo

Short Communication

Contact Info

Product

Resources

About

Amino-Acid Sequence of the α^D- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin