ABSTRACT. A novel method of chemistry applicable to the determination of trace lead in water samples based on the resonance light scattering (RLS) technique has been developed. In dilute phosphoric acid medium, in the presence of a large excess of I -, Pb(II) can form [PbI4] 2-, which further reacts with tetrabutyl ammonium bromide (TBAB) to form an ion-association compound. This results in significant enhancement of RLS intensity and the appearance of the corresponding RLS spectral characteristics. The maximum scattering peak of the system exists at 402 nm. Under optimum conditions, there is a linear relationship between the relative intensity of RLS and concentration of Pb(II) in the range of 0.04-1.8 µg/mL for the system with a low detection limit of 0.74 ng/mL for Pb(II). Based on this fact, a simple, rapid, and sensitive method has been developed for the determination of Pb(II) at nanogram level by RLS technique using a common spectrofluorimeter. This analytical system was successfully applied to determining trace amounts of Pb(II) in water samples that agree well with the results by atomic absorbance spectrometry (AAS).
The binding characteristics of the interaction between 3-(2-cyanoethyl) cytosine (CECT) and human serum albumin (HSA) were investigated using fluorescence, UV absorption spectroscopic and molecular modeling techniques under simulative physiological conditions. The intrinsic fluorescence intensity of HSA was decreased with the addition of CECT. The fluorescence data handled by Stern-Volmer equation proved that the quenching mechanism of the interaction between CECT and HSA was a static quenching procedure. The binding constants evaluated utilizing the Lineweaver-Burk equation at 17, 27 and 37 °C, were 2.340 × 10(4), 2.093 × 10(4) and 1.899 × 10(4) L mol(-1), respectively. The thermodynamic parameters were calculated according to van't Hoff equations. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic force played a major role in the binding process of CECT to HSA, which was consistent with the results of the molecular modeling study. In addition, the effect of other ions on the binding constant of CECT-HSA was examined.
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