2016
DOI: 10.1007/s00249-016-1121-6
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Thermal stability of extracellular hemoglobin of Rhinodrilus alatus (HbRa): DLS and SAXS studies

Abstract: Oxy-HbRa thermal stability was evaluated by dynamic light scattering (DLS) and small-angle X-ray scattering (SAXS) at pH 5.0, 7.0, 8.0, and 9.0. DLS results show that oxy-HbRa, at pH 7.0 and 5.0, remains stable up to 56 °C, undergoing denaturation/aggregation in acidic media above 60 °C, followed by partial sedimentation of aggregates. At alkaline pH values 8.0 and 9.0, oxy-HbRa oligomeric dissociation is observed above 30 °C, before denaturation. SAXS data show that oxy-HbRa, at 20 °C, is in its native form, … Show more

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Cited by 6 publications
(2 citation statements)
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“…The data reported in the current work and previous studies for HbGp and HbRa show that the ultracentrifugation above 50,000 rpm, followed by size exclusion chromatography (SEC), is an appropriate purification methodology for giant extracellular hemoglobins (Carvalho et al 2016;Santiago et al 2010). Analysis by the scattering particle number and volume (Fig.…”
Section: Dls Data Analysissupporting
confidence: 53%
“…The data reported in the current work and previous studies for HbGp and HbRa show that the ultracentrifugation above 50,000 rpm, followed by size exclusion chromatography (SEC), is an appropriate purification methodology for giant extracellular hemoglobins (Carvalho et al 2016;Santiago et al 2010). Analysis by the scattering particle number and volume (Fig.…”
Section: Dls Data Analysissupporting
confidence: 53%
“…In addition, the difference in terms of size when the vesicles were loaded (L) compared to the unloaded (UL) was not significant after each cycle of extrusion, indicating that the payload was not affecting the physical characteristics of the vesicles. Regarding the PdI values, which is a measure of the heterogeneity of a sample based on size, we had high values (about 0.5–0.6) owing to the presence of a small peak in all the samples, with a size of 6–7 nm that has been associated with the hemoglobin released by some cells that inevitably broke 36 , 37 . The raw product was then subjected to purification by ultracentrifugation (UC), and the final product was physically and biologically characterized by NTA, TEM, and FC.…”
Section: Resultsmentioning
confidence: 96%