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Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE

Apart from few early biophysical studies, the relative thermal instability of HbE has been only shown by clinical investigations. We have compared in vitro thermal stability of HbE with HbA(2) and HbA using optical spectroscopy. From absorption measurements in the soret region, synchronous fluoresce...

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Autores principales: Chakrabarti, Abhijit, Bhattacharya, Dipankar, Deb, Sanghamitra, Chakraborty, Madhumita
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828284/
https://www.ncbi.nlm.nih.gov/pubmed/24244748
http://dx.doi.org/10.1371/journal.pone.0081820
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author Chakrabarti, Abhijit
Bhattacharya, Dipankar
Deb, Sanghamitra
Chakraborty, Madhumita
author_facet Chakrabarti, Abhijit
Bhattacharya, Dipankar
Deb, Sanghamitra
Chakraborty, Madhumita
author_sort Chakrabarti, Abhijit
collection PubMed
description Apart from few early biophysical studies, the relative thermal instability of HbE has been only shown by clinical investigations. We have compared in vitro thermal stability of HbE with HbA(2) and HbA using optical spectroscopy. From absorption measurements in the soret region, synchronous fluorescence spectroscopy and dynamic light scattering experiments, we have found thermal stability of the three hemoglobin variants following the order HbE<HbA<HbA(2) in terms of structural unfolding and aggregation pattern. We have found formation of intermolecular dityrosine fluorophores with characteristic fluorescence signature, at pH >11.0 in all the three variants. Under oxidative stress conditions in presence of hydrogen peroxide, HbE has been found to be more vulnerable to aggregation compared to HbA and HbA(2). Taken together, these studies have shown thermal and oxidative instability of HbE and points towards the role of HbE in the upregulation of redox regulators and chaperone proteins in erythrocyte proteome of patients suffering from HbEbeta thalassemia.
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spelling pubmed-38282842013-11-16 Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE Chakrabarti, Abhijit Bhattacharya, Dipankar Deb, Sanghamitra Chakraborty, Madhumita PLoS One Research Article Apart from few early biophysical studies, the relative thermal instability of HbE has been only shown by clinical investigations. We have compared in vitro thermal stability of HbE with HbA(2) and HbA using optical spectroscopy. From absorption measurements in the soret region, synchronous fluorescence spectroscopy and dynamic light scattering experiments, we have found thermal stability of the three hemoglobin variants following the order HbE<HbA<HbA(2) in terms of structural unfolding and aggregation pattern. We have found formation of intermolecular dityrosine fluorophores with characteristic fluorescence signature, at pH >11.0 in all the three variants. Under oxidative stress conditions in presence of hydrogen peroxide, HbE has been found to be more vulnerable to aggregation compared to HbA and HbA(2). Taken together, these studies have shown thermal and oxidative instability of HbE and points towards the role of HbE in the upregulation of redox regulators and chaperone proteins in erythrocyte proteome of patients suffering from HbEbeta thalassemia. Public Library of Science 2013-11-14 /pmc/articles/PMC3828284/ /pubmed/24244748 http://dx.doi.org/10.1371/journal.pone.0081820 Text en © 2013 Chakrabarti et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Chakrabarti, Abhijit
Bhattacharya, Dipankar
Deb, Sanghamitra
Chakraborty, Madhumita
Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title_full Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title_fullStr Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title_full_unstemmed Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title_short Differential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA(2) and HbE
title_sort differential thermal stability and oxidative vulnerability of the hemoglobin variants, hba(2) and hbe
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828284/
https://www.ncbi.nlm.nih.gov/pubmed/24244748
http://dx.doi.org/10.1371/journal.pone.0081820
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