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Silva,D.; Cortez,C.M.; Louro,S.R.W.. |
The binding of chlorpromazine (CPZ) and hemin to bovine serum albumin was studied by the fluorescence quenching technique. CPZ is a widely used anti-psychotic drug that interacts with blood components, influences bioavailability, and affects function of several biomolecules. Hemin is an important ferric residue of hemoglobin that binds within the hydrophobic region of albumin with high specificity. Quenching of the intrinsic fluorescence of bovine serum albumin (BSA) was observed by selectively exciting tryptophan residues at 290 nm. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern-Volmer graphs were plotted, and the quenching constant estimated for BSA solution titrated with hemin at 25ºC was 1.44 (± 0.05) x... |
Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Chlorpromazine; Hemin; Albumin; Fluorescence quenching. |
Ano: 2004 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000700004 |