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[Relation between fluorescence and circular dichroism of the complex of the fluorescence probe 4-dimethylaminochalcone with serum albumin].
Metadata
JournalBiofizikaNot FoundDate
1975-Jul-Aug
Publication Type
Journal Article
English Abstract
Volume
1975-Jul-Aug / 20 : 581-5
Author
Dobretsov GE , Kharitonenkov IG , Mishiev VE , Vladimirov IuA
Doi
Not Found
PMIDMESH
Chalcone
Circular Dichroism
Humans
Hydrogen-Ion Concentration
Propiophenones
Serum Albumin
Spectrometry, Fluorescence
Abstract
The fluorescence probe(4-dimethylaminochalcone; DMH) was noncovalently linked to human serum albumin (HSA). The variation of pH was due to serum albumin structural changes, which was determined in terms of DMH and HSA fluorescence and CD spectra. Considerable changes of fluorescence and CD spectra were observed at pH 8 and 10, where there is ionization of two more recently titrated tyrosin residues. It is assumed that these two tyrosine residues are in binding region and quench the fluorescence of DMH between pH 4 to 8. Quenching disappears if these residues are ionized (pH greater than 8) or if the protein undergoes the N -F transition (pH less than 4).
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