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Number of results

Journal

2011 | 9 | 2 | 245-252

Article title

Evidence of changes in hydrophilic/hydrophobic balance and in chemical activity of HSA induced by thermal treatments

Content

Title variants

Languages of publication

EN

Abstracts

EN
Samples of human serum albumin (HSA) obtained as a result of heat denaturation followed by refolding controlled by a cooling of the protein solution were studied by several methods: chromatographic measurements, kinetic of the reaction with a water soluble free radical and by electron paramagnetic resonance (EPR) spectroscopy. In this context the interaction of this protein with β-cyclodextrin (β-CD) and sodium dodecyl sulfate (SDS) was also investigated. Reversed phase thin layer chromatography (RP-TLC) showed changes in lipophylicity of HSA, which are related with the existence of different ensembles of conformers. The UV-Vis absorption spectra had shown the broadening of absorption band of the protein and a hyperchrom effect in the presence of SDS; β-CD reduces the effect of SDS on protein UV-Vis spectra.Kinetic measurements related to the reaction of HSA with a water soluble DPPH type free radical provided evidence that reactivity of the HSA denaturated conformers is higher compared with the natural conformer. The affinity of SDS to the albumins surface and the effect of β-CD on the SDS/protein aggregates were also evident by changes in the EPR spectra of the spin probe CAT16.

Publisher

Journal

Year

Volume

9

Issue

2

Pages

245-252

Physical description

Dates

published
1 - 4 - 2011
online
17 - 2 - 2011

Contributors

author
  • University of Bucharest
  • Romanian Academy

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.-psjd-doi-10_2478_s11532-010-0148-2
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