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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Main Authors: Yuan, Yue, Tong-Jian Shen, Priyamvada Gupta, Ho, Nancy T., Simplaceanu, Virgil, Tsuey Chyi Tam, Hofreiter, Michael, Cooper, Alan, Campbell, Kevin L., Ho, Chien
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Published: Carnegie Mellon University 2011
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Online Access: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
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spelling 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
institution Open Polar
collection DataCite Metadata Store (German National Library of Science and Technology)
op_collection_id ftdatacite
language unknown
topic 69999 Biological Sciences not elsewhere classified
FOS Biological sciences
spellingShingle 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
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