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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Bibliographic Details
Main Authors: Yue Yuan, Tong-Jian Shen, Priyamvada Gupta, Nancy T. Ho, Virgil Simplaceanu, Tsuey Chyi Tam, Michael Hofreiter, Alan Cooper, Kevin L. Campbell, Chien Ho
Format: Other Non-Article Part of Journal/Newspaper
Language:unknown
Published: 2018
Subjects:
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
Arctic
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
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Summary: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.

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