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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Guanidine hydrochloride and urea effects upon thermal stability of Glossoscolex paulistus hemoglobin (HbGp)

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Author(s):
Carvalho, Francisco A. O. [1] ; Alves, Fernanda R. [1] ; Carvalho, Jose W. P. [1, 2] ; Tabak, Marcel [1]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Inst Quim Sao Carlos, BR-05508 Sao Paulo - Brazil
[2] Univ Estado Mato Grosso, Caceres, MT - Brazil
Total Affiliations: 2
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 74, p. 18-28, MAR 2015.
Web of Science Citations: 8
Abstract

Glossoscolex paulistus hemoglobin (HbGp) has a molecular mass of 3600 kDa. It belongs to the hexagonal bilayer hemoglobin class, which consists of highly cooperative respiratory macromolecules found in mollusks and annelids. The present work focusses on oxy-HbGp thermal stability, in the presence of urea and guanidine hydrochloride (GuHCI), monitored by several techniques. Initially, dynamic light scattering data show that the presence of GuHCI induces the protein oligomeric dissociation, followed by a significant 11-fold increase in the hydrodynamic diameter (D-H) values, due to the formation of protein aggregates in solution. In contrast, urea promotes the HbGp oligomeric dissociation, followed by unfolding process at high temperatures, without aggregation. Circular dichroism data show that unfolding critical temperature (T-c) of oxy-HbGp decreases from 57 degrees C, at 0.0 mol/L of the denaturant, to 45 degrees C, in the presence of 3.5 mol/L of urea, suggesting the reduction of HbGp oligomeric stability. Moreover, differential scanning calorimetry results show that at lower GuHC1 concentrations, some thermal stabilization of the hemoglobin is observed, whereas at higher concentrations, the reduction of stability takes place. Besides, HbGp is more stable in the presence of urea when compared with the guanidine effect, as deduced from the differences in the concentration range of denaturants. (C) 2014 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 11/09863-6 - Analysis of giant extracellular hemoglobin from Glossoscolex paulistus (HbGp) and ionic surfactants interaction by isothermal titration calorimetry
Grantee:Fernanda Rosa Alves
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 13/09349-6 - Thermal and kinetic stability of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp): effects of surfactants, salts, urea, iron heme oxidation state and pH.
Grantee:José Wilson Pires Carvalho
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 13/09829-8 - Biophysical and structural studies of extracellular hemoglobin of Glossoscolex paulistus, and its monomer d and dodecamer (abcd)3 subunits.
Grantee:Francisco Adriano de Oliveira Carvalho
Support Opportunities: Scholarships in Brazil - Post-Doctoral