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dc.contributor.authorGałęcki, Krystian
dc.contributor.authorDespotović, Biljana
dc.contributor.authorGalloway, Celine
dc.contributor.authorIoannidis, Angelos-Gerasimos
dc.contributor.authorJanani, Tahereh
dc.contributor.authorNakamura, Yuki
dc.contributor.authorOluyinka, Grace
dc.date.accessioned2015-06-03T11:11:22Z
dc.date.available2015-06-03T11:11:22Z
dc.date.issued2012
dc.identifier.citationBiotechnology and Food Science, 2012 Vol.76 nr 1 s.3-12
dc.identifier.issn2084-0136
dc.identifier.other0000039430
dc.identifier.urihttp://hdl.handle.net/11652/278
dc.description.abstractThe 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)x104M-1and (4.32±0.30)x104M-1for 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 (kqT)of the proteins studied by harmane was (1.15± 0.10)x107M-1s-1and (2.88±0.22)x107M-1s-1for HSA and BSA, respectively. Based on the similar value of K and kqTfor 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.en_EN
dc.formatapplication/pdf
dc.language.isoenen_EN
dc.publisherWydawnictwo Politechniki Łódzkiejpl_PL
dc.publisherLodz University of Technology. Pressen_EN
dc.relation.ispartofseriesZeszyty Naukowe Politechniki Łódzkiejpl_PL
dc.relation.ispartofseriesBiotechnology and Food Scienceen_EN
dc.titleBinding of harmane to human and bovine serum albumin: fluorescence and phosphorescence studyen_EN
dc.typeArticleen_EN
dc.typeArtykułpl_PL


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