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Literature DB >> 3255379

Primary structure of the hemoglobin alpha-chain of rose-ringed parakeet (Psittacula krameri).

A Islam¹, O U Beg, B Persson, Z H Zaidi, H Jörnvall.

Abstract

The structure of the hemoglobin alpha-chain of Rose-ringed Parakeet was determined by sequence degradations of the intact subunit, the CNBr fragments, and peptides obtained by digestion with staphylococcal Glu-specific protease and trypsin. Using this analysis, the complete alpha-chain structure of 21 avian species is known, permitting comparisons of the protein structure and of avian relationships. The structure exhibits differences from previously established avian alpha-chains at a total of 61 positions, five of which have residues unique to those of the parakeet (Ser-12, Gly-65, Ser-67, Ala-121, and Leu-134). The analysis defines hemoglobin variation within an additional avian order (Psittaciformes), demonstrates distant patterns for evaluation of relationships within other avian orders, and lends support to taxonomic conclusions from molecular data.

Entities: Chemical Species

Mesh：

Substances：
Amino Acids
Hemoglobins

Year: 1988 PMID： 3255379 DOI： 10.1007/bf01024874

Source DB: PubMed Journal: J Protein Chem ISSN： 0277-8033

24 in total

1. Amino acid sequence and immunological properties of chalchalaca egg white lysozyme.

Authors: J Jollès; F Schoentgen; P Jollès; E M Prager; A C Wilson
Journal: J Mol Evol Date: 1976-06-23 Impact factor: 2.395

2. Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes.

Authors: R Kaiser; B Holmquist; J Hempel; B L Vallee; H Jörnvall
Journal: Biochemistry Date: 1988-02-23 Impact factor: 3.162

3. Penguin hemoglobin (Aptenodytes forsteri). A 45 residue N-terminal sequence.

Authors: C Monier; A G Schnek; J Dirkx; J Leonis
Journal: FEBS Lett Date: 1973-10-01 Impact factor: 4.124

4. No evidence for 'stress' alpha-globin genes in chicken.

Authors: W Knöchel; B Wittig; S Wittig; M E John; U Grundmann; W Oberthür; J Godovac; G Braunitzer
Journal: Nature Date: 1982-02-25 Impact factor: 49.962

5. The amino acid sequence of Canada goose (Branta canadensis) and mute swan (Cygnus olor) hemoglobins. Two different species with identical beta-chains.

Authors: W Oberthür; J Godovac-Zimmermann; G Braunitzer; H Wiesner
Journal: Hoppe Seylers Z Physiol Chem Date: 1982-08

6. [Hemoglobins of thecommon starling (Sturnus vulgaris, Passeriformes). The primary structures of the alphaA, alphaD and beta chains].

Authors: W Oberthür; G Braunitzer
Journal: Hoppe Seylers Z Physiol Chem Date: 1984-02

7. The amino-acid sequence of Northern Mallard (Anas platyrhynchos platyrhynchos) hemoglobin.

Authors: J Godovac-Zimmermann; G Braunitzer
Journal: Hoppe Seylers Z Physiol Chem Date: 1983-06

8. The primary structure of alpha A- and beta-chains from blue-and-yellow macaw (Ara ararauna, Psittaci) hemoglobin. No evidence for expression of alpha D-chains.

Authors: J Godovac-Zimmermann; G Braunitzer
Journal: Biol Chem Hoppe Seyler Date: 1985-05

9. [Hemoglobins, XLVII. Hemoglobins of the bar-headed goose (Anser indicus): primary structure and physiology of respiration, systematic and evolution].

Authors: W Oberthür; G Braunitzer; I Würdinger
Journal: Hoppe Seylers Z Physiol Chem Date: 1982-06

10. Ovomucoid third domains from 100 avian species: isolation, sequences, and hypervariability of enzyme-inhibitor contact residues.

Authors: M Laskowski; I Kato; W Ardelt; J Cook; A Denton; M W Empie; W J Kohr; S J Park; K Parks; B L Schatzley
Journal: Biochemistry Date: 1987-01-13 Impact factor: 3.162

5 in total

Primary structure of the hemoglobin alpha-chain of rose-ringed parakeet (Psittacula krameri).

1. Amino acid sequence and immunological properties of chalchalaca egg white lysozyme.

2. Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes.

3. Penguin hemoglobin (Aptenodytes forsteri). A 45 residue N-terminal sequence.

4. No evidence for 'stress' alpha-globin genes in chicken.

5. The amino acid sequence of Canada goose (Branta canadensis) and mute swan (Cygnus olor) hemoglobins. Two different species with identical beta-chains.

6. [Hemoglobins of thecommon starling (Sturnus vulgaris, Passeriformes). The primary structures of the alphaA, alphaD and beta chains].

7. The amino-acid sequence of Northern Mallard (Anas platyrhynchos platyrhynchos) hemoglobin.

8. The primary structure of alpha A- and beta-chains from blue-and-yellow macaw (Ara ararauna, Psittaci) hemoglobin. No evidence for expression of alpha D-chains.

9. [Hemoglobins, XLVII. Hemoglobins of the bar-headed goose (Anser indicus): primary structure and physiology of respiration, systematic and evolution].

10. Ovomucoid third domains from 100 avian species: isolation, sequences, and hypervariability of enzyme-inhibitor contact residues.

1. Primary structure of hemoglobin beta-chain from Columba livia (gray wild pigeon).

2. Primary structure of hemoglobin from gray partridge (Francolinus pondacerianus, Galliformes).

3. Primary structure of hemoglobin alpha-chain of Columba livia (gray wild pigeon).

4. Primary structure of the hemoglobin beta-chain of rose-ringed parakeet (Psittacula krameri).

5. Primary structure of hemoglobin alpha-chain from cuckoo (Eudynamys scolopaceae, cuculiformes).