Open AccessDifferential Thermal Stability and Oxidative Vulnerability of the Hemoglobin Variants, HbA2 and HbE
Author(s) -
Abhijit Chakrabarti,
Dipankar Bhattacharya,
Sanghamitra Deb,
M. Chakraborty
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0081820
Subject(s) - hemoglobin , chemistry , biophysics , oxidative phosphorylation , oxidative stress , chaperone (clinical) , hemoglobin e , biochemistry , biology , medicine , pathology
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 HbE11.0 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.