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2012 | z. 76, nr 1 | 3--12
Tytuł artykułu

Binding of Harmane to Human and Bovine Serum Albumin: Fluorescence and Phosphorescence Study

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The binding of harmane with human serum albumin (HSA) and bovine serum albumin (BSA) were studied by fluorescence and phosphorescence spectroscopic methods. Quenching of fluorescence of serum albumins by harmane was found to be a static quenching process. The equilibrium constant (K) of complex formation was found to be equal to (5.16±0.28)x104 M-1 and (4.32±0.30)x104 M-1 for HSA and BSA, respectively. It was found that the interactions of harmane with HSA and BSA were also in the excited triplet state. The determined bimolecular constant or triplet state quenching (kqƬ)of the proteins studied by harmane was (1.15± 0.10)x107 M-1 s-1 and (2.88±0.22)x107 M-1 s-1 for HSA and BSA, respectively. Based on the similar value of K and kq Ƭ for HSA and BSA, a possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa. (original abstract)
Rocznik
Numer
Strony
3--12
Opis fizyczny
Twórcy
  • Lodz University of Technology, Poland
  • University of Sarajevo, Bosnia and Herzegovina
  • University of Newcastle Upon Tyne, England
  • Agricultural University of Athens, Greece
  • Norwegian University of Science and Technology, Trondheim, Norway
  • Kyushu University, Fukuoka, Japan
  • University of Greenwich, London, England
Bibliografia
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Typ dokumentu
Bibliografia
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