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...
Main Authors: | , , , , , , , , , |
---|---|
Format: | Other Non-Article Part of Journal/Newspaper |
Language: | unknown |
Published: |
2018
|
Subjects: | |
Online Access: | https://doi.org/10.1184/r1/6097031.v1 https://figshare.com/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031 |
id |
ftcarnmellonufig:oai:figshare.com:article/6097031 |
---|---|
record_format |
openpolar |
spelling |
ftcarnmellonufig:oai:figshare.com:article/6097031 2023-05-15T15:13:54+02:00 A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. Yue Yuan Tong-Jian Shen Priyamvada Gupta Nancy T. Ho Virgil Simplaceanu Tsuey Chyi Tam Michael Hofreiter Alan Cooper Kevin L. Campbell Chien Ho 2018-04-05T09:11:46Z https://doi.org/10.1184/r1/6097031.v1 https://figshare.com/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031 unknown doi:10.1184/r1/6097031.v1 https://figshare.com/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031 In Copyright Biological Sciences not elsewhere classified Alkanesulfonic Acids Amino Acid Sequence Animals Biophysical Processes Blood Substitutes Buffers Elephants Hemoglobin A2 Hemoglobins Humans Hydrogen-Ion Concentration Mammoths Molecular Sequence Data Morpholines Oxygen Phosphates Temperature Text Journal contribution 2018 ftcarnmellonufig https://doi.org/10.1184/r1/6097031.v1 2019-11-18T10:43:16Z 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. Other Non-Article Part of Journal/Newspaper Arctic KiltHub Research from Carnegie Mellon University Arctic |
institution |
Open Polar |
collection |
KiltHub Research from Carnegie Mellon University |
op_collection_id |
ftcarnmellonufig |
language |
unknown |
topic |
Biological Sciences not elsewhere classified Alkanesulfonic Acids Amino Acid Sequence Animals Biophysical Processes Blood Substitutes Buffers Elephants Hemoglobin A2 Hemoglobins Humans Hydrogen-Ion Concentration Mammoths Molecular Sequence Data Morpholines Oxygen Phosphates Temperature |
spellingShingle |
Biological Sciences not elsewhere classified Alkanesulfonic Acids Amino Acid Sequence Animals Biophysical Processes Blood Substitutes Buffers Elephants Hemoglobin A2 Hemoglobins Humans Hydrogen-Ion Concentration Mammoths Molecular Sequence Data Morpholines Oxygen Phosphates Temperature Yue Yuan Tong-Jian Shen Priyamvada Gupta Nancy T. Ho Virgil Simplaceanu Tsuey Chyi Tam Michael Hofreiter Alan Cooper Kevin L. Campbell Chien Ho A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. |
topic_facet |
Biological Sciences not elsewhere classified Alkanesulfonic Acids Amino Acid Sequence Animals Biophysical Processes Blood Substitutes Buffers Elephants Hemoglobin A2 Hemoglobins Humans Hydrogen-Ion Concentration Mammoths Molecular Sequence Data Morpholines Oxygen Phosphates Temperature |
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 |
Other Non-Article Part of Journal/Newspaper |
author |
Yue Yuan Tong-Jian Shen Priyamvada Gupta Nancy T. Ho Virgil Simplaceanu Tsuey Chyi Tam Michael Hofreiter Alan Cooper Kevin L. Campbell Chien Ho |
author_facet |
Yue Yuan Tong-Jian Shen Priyamvada Gupta Nancy T. Ho Virgil Simplaceanu Tsuey Chyi Tam Michael Hofreiter Alan Cooper Kevin L. Campbell Chien Ho |
author_sort |
Yue Yuan |
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. |
publishDate |
2018 |
url |
https://doi.org/10.1184/r1/6097031.v1 https://figshare.com/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_relation |
doi:10.1184/r1/6097031.v1 https://figshare.com/articles/A_biochemical--biophysical_study_of_hemoglobins_from_woolly_mammoth_Asian_elephant_and_humans_/6097031 |
op_rights |
In Copyright |
op_doi |
https://doi.org/10.1184/r1/6097031.v1 |
_version_ |
1766344413144940544 |