Darwinian evolution in the genealogy of haemoglobin

Goodman, Miriam B.; Gw, Moore; Matsuda, Genji

doi:10.1038/253603a0

Cited by 293 publications

(148 citation statements)

References 67 publications

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“…Goodman et al (6), observing the homology between the ␣ and ␤ chains of hemoglobin, hypothesized that the ancestral hemoglobin molecule, before the gene duplication that gave rise to separate ␣ and ␤ chain genes, was a homotetramer. Jensen (7), observing the ''substrate ambiguity'' of many contemporary enzymes, proposed that after duplication of an ancestral gene encoding an enzyme of broad specificity, the daughter genes may divide the work of the ancestor, encoding enzymes of narrower specificity.…”

Section: New Proteins For Old Functionsmentioning

confidence: 99%

Gene duplication and the origin of novel proteins

Hughes

2005

Proc. Natl. Acad. Sci. U.S.A.

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Section: New Proteins For Old Functionsmentioning

confidence: 99%

Gene duplication and the origin of novel proteins

Hughes

2005

Proc. Natl. Acad. Sci. U.S.A.

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“…For residue positions with defined functional roles in mammalian a-and /3-chains of haemoglobin in connection with the Bohr effect, binding of polyphosphates such as 2,3-diphosphoglycerate, or salt links between the chains in tetramers (Goodman et al 1975), there are no identical positions when compared with human haemoglobin chains. This is in keeping with the absence ofheterotropic interactions in the dimeric haemoglobin (Furuta et al 1980).…”

Section: Discussionmentioning

confidence: 99%

Amino Acid Sequence of the Globin lIB Chain of the Dimeric Haemoglobin of the Bivalve Mollusc Andara trapezia

Wk¹,

Gilbert²,

Thompson³

1984

Aust. Jnl. Of Bio. Sci.

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The tryptic peptides of the S-carboxymethylated globin chain ofa dimeric haemoglobin from A. trapezia were purified by high-performance liquid chromatography and their amino acid sequences determined by the dansyl-Edman method.The cyanogen bromide fragments were purified or digested with chymotrypsin to give overlap fragments which were sequenced by similar methods.In conjunction with some sequences of larger peptides derived by digestion with staphylococal protease, the complete sequence of 146 residues was deduced. The sequence has been compared with that previously determined for the 153 residue a-chain of the tetrameric haemoglobin from the same mollusc and shows 45% identity. In the E and F helical regions the homology is particularly noticeable with 75 and 100% identity respectively. The sequence of the dimeric haemoglobin chain of A. trazezia is very homologous (90% identity) to the published sequence of the similar haemoglobin from A. broughtonU. The homology when compared with other globin chains is much less, with approximately 20% identity in amino acid sequence.

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“…Significant amino acid differences in echidna and platypus haemoglobins Sequence data are from Whittaker et al (1972Whittaker et al ( , 1973, and Whittaker and Thompson (1974). The functional significance is from Goodman et al (1975) to have sufficiently similar stereochemical properties that they are unlikely to have a significant effect. In the oc-chains the substitutions CD4 Met --+ Phe and EI0 Arg --+ Lys are involved in important haem contacts (Perutz 1976), and although the residues have similar chemical properties th~.ir steric differences, although minor, could well modify the relation between the haem and the CD and E helices.…”

Section: Discussionmentioning

confidence: 99%

“…The amino acid sequence studies show 16 amino acid differences between the ~-chain of echidna Hb-IB and platypus haemoglobin and 14 amino acid differences between the ,8~chains. Goodman et al (1975) have listed amino acid residues with defined functional roles in mammalian haemoglobin oc-and ,8-chains. It might be expected that the marked differences in oxygen binding properties between echidna and platypus haemoglobins are due to amino acid substitutions at sites having known functional roles, However, the important OC1,82 contact sites, DPG binding sites, and residues involved in the Bohr effect are identical in platypus and echidna haemoglobin.…”

Section: Discussionmentioning

confidence: 99%

Oxygen Binding of Monotreme Haemoglobins I. Oxygen Binding Parameters of the Haemoglobins of Platypus, Ornithorhynchus anatinus, and Echidna, Tachyglossus aculeatus

Hosken¹

1978

Aust. Jnl. Of Bio. Sci.

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Oxygen binding parameters have been determined for echidna and platypus haemolysates. At pH 7· 1 and 25°C platypus haemoglobin with an oxygen half-saturation pressure (Pso) of 2·4 kPa has a lower oxygen affinity than echidna haemoglobin with a Pso of 1·6 kPa. The AH o of oxygenation of platypus haemoglobin is -38·9kJ/mol which is more exothermic than the -29·7kJ/mol of echidna haemoglobin. Platypus haemoglobin has a steeper alkaline Bohr curve than echidna haemoglobin, while both haemoglobins show high levels of cooperativity at various temperatures and pH values. It appears that diphosphoglyceric acid modulates the affinity of echidna and platypus haemoglobins to different extents. This information is interpreted in terms of the steric effects of ligand binding originating in the amino acid sequence differences of these two species.

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Darwinian evolution in the genealogy of haemoglobin

Cited by 293 publications

References 67 publications

Gene duplication and the origin of novel proteins

Gene duplication and the origin of novel proteins

Amino Acid Sequence of the Globin lIB Chain of the Dimeric Haemoglobin of the Bivalve Mollusc Andara trapezia

Oxygen Binding of Monotreme Haemoglobins I. Oxygen Binding Parameters of the Haemoglobins of Platypus, Ornithorhynchus anatinus, and Echidna, Tachyglossus aculeatus

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