Thermal stability of extracellular hemoglobin of Glossoscolex paulistus: Determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies

Santiago, Patrícia S.; Carvalho, José Wilson Pires; Domingues, Marco M.; Santos, Nuno C.; Tabak, Marcel

doi:10.1016/j.bpc.2010.08.010

Cited by 27 publications

(29 citation statements)

References 25 publications

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“…Moreover, other hydrodynamic properties, shown in Table 1, such as the MM of 3600 ± 100 kDa, and the Stokes radius (R S ) of 13.5 ± 0.2 nm, suggest that the species present at 1.0 mol/L of urea is indeed undissociated oxy-HbGp. The R S value estimated for oxyHbGp by AUC is very consistent with the hydrodynamic diameter value (D h ) of 27 ± 1 nm, determined independently by DLS studies [3]. The MM values shown in Table 1 were obtained by the global analysis of the sedimentation velocity data (SV) using the SEDPHAT software (version 9.4).…”

Section: Auc Datamentioning

confidence: 99%

“…These extracellular hemoglobins are characterized by a very high molecular mass (MM), a high resistance to oxidation and a high oligomeric stability when subjected to conditions of stress such as high temperature, pH variation, and addition of chemical agents, such as urea and surfactants [3][4][5][6], as compared, for instance, with human hemoglobin. These properties make them an interesting and important system for investigation [2,7], including in biomedical applications.…”

Section: Introductionmentioning

confidence: 99%

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Urea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model

Carvalho

Santiago

et al. 2013

International Journal of Biological Macromolecules

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The urea effect on the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) stability was studied by analytical ultracentrifugation (AUC) and small angle X-ray scattering (SAXS). AUC data show that the sedimentation coefficient distributions curves c (S), at 1.0 mol/L of urea, display a single peak at 57 S, associated to the undissociated protein. The increase in urea concentration, up to 4.0 mol/L, induces the appearance of smaller species, due to oligomeric dissociation. The sedimentation coefficients and molecular masses are 9.2S and 204 kDa for the dodecamer (abcd)(3), 5.5S and 69 kDa for the tetramer (abcd), 4.1S and 52 kDa for the trimer (abc) and 2.0 S and 17 kDa for the monomer d, respectively. SAXS data show initially a decrease in the I(0) values due to the oligomeric dissociation, and then, above 4.0 mol/L of denaturant, for oxy-HbGp, and above 6.0 mol/L for cyanomet-HbGp, an increase in the maximum dimension and gyration radius is observed, due to the unfolding process. According to AUC and SAXS data the HbGp unfolding is described by two phases: the first one, at low urea concentration, below 4.0 mol/L, characterizes the oligomeric dissociation, while the second one, at higher urea concentration, is associated to the unfolding of dissociated species. Our results are complementary to a recent report based on spectroscopic observations.

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Section: Auc Datamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Urea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model

Carvalho

Santiago

et al. 2013

International Journal of Biological Macromolecules

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“…They are characterized by a very high molecular mass (MM) around 3500 kDa [2,3], a high resistance to auto-oxidation [4] and a high oligomeric stability, when exposed to different conditions of stress, such as, high temperature [5,6], pH variation [7], and addition of chemical agents [8][9][10]. The extracellular hemoglobin of Glossoscolex paulistus (HbGp) has a molecular mass of 3.6 MDa [11], and its oligomeric structure is composed by 144 globin chains, and 36 additional chains lacking the heme group, named linkers [12,13].…”

Section: Introductionmentioning

confidence: 99%

Metals content of Glossoscolex paulistus extracellular hemoglobin: Its peroxidase activity and the importance of these ions in the protein stability

Caruso

Biazin

Carvalho

et al. 2016

Journal of Inorganic Biochemistry

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“…The analogous change in DSC profiles with varying protein concentrations were obtained for other dissociating protein Residues and structural elements of the subunit A′ are designated by primes. The figure is generated by using the MolBrowser 3.8-4a software (MolSoft) (Surolia et al 1996), winged bean acidic lectin (Srinivas et al 1998), Phb from rabbit skeletal muscles , filamentous actin (Mikhailova et al 2006), Entamoeba histolytica triosephosphate isomerase (Tellez et al 2008) and extracellular hemoglobin of Glossoscolex paulistus (Santiago et al 2010). …”

Section: Dissociative Mechanism For Irreversible Thermal Denaturationmentioning

confidence: 99%

Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

2016

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Protein stability is a fundamental characteristic essential for understanding conformational transformations of the proteins in the cell. When using protein preparations in biotechnology and biomedicine, the problem of protein stability is of great importance. The kinetics of denaturation of oligomeric proteins may have characteristic properties determined by the quaternary structure. The kinetic schemes of denaturation can include the multiple stages of conformational transitions in the protein oligomer and stages of reversible dissociation of the oligomer. In this case, the shape of the kinetic curve of denaturation or the shape of the melting curve registered by differential scanning calorimetry can vary with varying the protein concentration. The experimental data illustrating dissociative mechanism for irreversible thermal denaturation of oligomeric proteins have been summarized in the present review. The use of test systems based on thermal aggregation of oligomeric proteins for screening of agents possessing anti-aggregation activity is discussed.

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Thermal stability of extracellular hemoglobin of Glossoscolex paulistus: Determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies

Cited by 27 publications

References 25 publications

Urea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model

Urea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model

Metals content of Glossoscolex paulistus extracellular hemoglobin: Its peroxidase activity and the importance of these ions in the protein stability

Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

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