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2011 | 9 | 2 | 245-252
Tytuł artykułu

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

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
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.
Wydawca

Czasopismo
Rocznik
Tom
9
Numer
2
Strony
245-252
Opis fizyczny
Daty
wydano
2011-04-01
online
2011-02-17
Twórcy
  • University of Bucharest
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Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_2478_s11532-010-0148-2
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