A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans.
This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional...
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2011
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ftdatacite:10.1184/r1/6097031.v1 2023-05-15T15:10:16+02:00 A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. Yuan, Yue Tong-Jian Shen Priyamvada Gupta Ho, Nancy T. Simplaceanu, Virgil Tsuey Chyi Tam Hofreiter, Michael Cooper, Alan Campbell, Kevin L. Ho, Chien 2011 https://dx.doi.org/10.1184/r1/6097031.v1 https://kilthub.cmu.edu/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031/1 unknown Carnegie Mellon University https://dx.doi.org/10.1184/r1/6097031 In Copyright http://rightsstatements.org/vocab/InC/1.0/ 69999 Biological Sciences not elsewhere classified FOS Biological sciences Text article-journal Journal contribution ScholarlyArticle 2011 ftdatacite https://doi.org/10.1184/r1/6097031.v1 https://doi.org/10.1184/r1/6097031 2021-11-05T12:55:41Z This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional properties of recombinant hemoglobins (rHb) from woolly mammoth (rHb WM) and Asian elephant (rHb AE) in relation to human hemoglobins Hb A and Hb A(2) (a minor component of human blood). We have obtained oxygen equilibrium curves and calculated O(2) affinities, Bohr effects, and the apparent heat of oxygenation (ΔH) in the presence and absence of allosteric effectors [inorganic phosphate and inositol hexaphosphate (IHP)]. Here, we show that the four Hbs exhibit distinct structural properties and respond differently to allosteric effectors. In addition, the apparent heat of oxygenation (ΔH) for rHb WM is less negative than that of rHb AE, especially in phosphate buffer and the presence of IHP, suggesting that the oxygen affinity of mammoth blood was also less sensitive to temperature change. Finally, (1)H NMR spectroscopy data indicates that both α(1)(β/δ)(1) and α(1)(β/δ)(2) interfaces in rHb WM and rHb AE are perturbed, whereas only the α(1)δ(1) interface in Hb A(2) is perturbed compared to that in Hb A. The distinct structural and functional features of rHb WM presumably facilitated woolly mammoth survival in the Arctic environment. Text Arctic DataCite Metadata Store (German National Library of Science and Technology) Arctic |
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69999 Biological Sciences not elsewhere classified FOS Biological sciences |
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69999 Biological Sciences not elsewhere classified FOS Biological sciences Yuan, Yue Tong-Jian Shen Priyamvada Gupta Ho, Nancy T. Simplaceanu, Virgil Tsuey Chyi Tam Hofreiter, Michael Cooper, Alan Campbell, Kevin L. Ho, Chien A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
topic_facet |
69999 Biological Sciences not elsewhere classified FOS Biological sciences |
description |
This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional properties of recombinant hemoglobins (rHb) from woolly mammoth (rHb WM) and Asian elephant (rHb AE) in relation to human hemoglobins Hb A and Hb A(2) (a minor component of human blood). We have obtained oxygen equilibrium curves and calculated O(2) affinities, Bohr effects, and the apparent heat of oxygenation (ΔH) in the presence and absence of allosteric effectors [inorganic phosphate and inositol hexaphosphate (IHP)]. Here, we show that the four Hbs exhibit distinct structural properties and respond differently to allosteric effectors. In addition, the apparent heat of oxygenation (ΔH) for rHb WM is less negative than that of rHb AE, especially in phosphate buffer and the presence of IHP, suggesting that the oxygen affinity of mammoth blood was also less sensitive to temperature change. Finally, (1)H NMR spectroscopy data indicates that both α(1)(β/δ)(1) and α(1)(β/δ)(2) interfaces in rHb WM and rHb AE are perturbed, whereas only the α(1)δ(1) interface in Hb A(2) is perturbed compared to that in Hb A. The distinct structural and functional features of rHb WM presumably facilitated woolly mammoth survival in the Arctic environment. |
format |
Text |
author |
Yuan, Yue Tong-Jian Shen Priyamvada Gupta Ho, Nancy T. Simplaceanu, Virgil Tsuey Chyi Tam Hofreiter, Michael Cooper, Alan Campbell, Kevin L. Ho, Chien |
author_facet |
Yuan, Yue Tong-Jian Shen Priyamvada Gupta Ho, Nancy T. Simplaceanu, Virgil Tsuey Chyi Tam Hofreiter, Michael Cooper, Alan Campbell, Kevin L. Ho, Chien |
author_sort |
Yuan, Yue |
title |
A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
title_short |
A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
title_full |
A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
title_fullStr |
A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
title_full_unstemmed |
A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
title_sort |
biochemical--biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans. |
publisher |
Carnegie Mellon University |
publishDate |
2011 |
url |
https://dx.doi.org/10.1184/r1/6097031.v1 https://kilthub.cmu.edu/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031/1 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_relation |
https://dx.doi.org/10.1184/r1/6097031 |
op_rights |
In Copyright http://rightsstatements.org/vocab/InC/1.0/ |
op_doi |
https://doi.org/10.1184/r1/6097031.v1 https://doi.org/10.1184/r1/6097031 |
_version_ |
1766341311816794112 |