Jul 1, 1975

Relation between fluorescence and circular dichroism of the complex of the fluorescence probe 4-dimethylaminochalcone with serum albumin

G E DobretsovIu A Vladimirov


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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Mentioned in this Paper

Serum Albumin Measurement
Albumin Human, USP
Human Serum Albumin [EPC]
Fluorescence Spectroscopy
Plasma Albumin
Circular Dichroism, Vibrational
Tyrosine Measurement

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