Journal
CHROMATOGRAPHIA
Volume 71, Issue 11-12, Pages 1075-1079Publisher
SPRINGER HEIDELBERG
DOI: 10.1365/s10337-010-1573-2
Keywords
Column liquid chromatography; Microdialysis; Human serum albumin; As-III and As-V
Funding
- national Science Foundation of China [30530640]
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Study on the stoichiometry and affinity of the arsenicals bound to HSA is an important step toward a better understanding of arsenic toxic effects. After incubation of As-III or As-V with HSA at the physiological conditions (pH 7.43 and 37 A degrees C), the free arsenicals and arsenic-HSA complexes were separated and detected by the combined techniques of microdialysis and liquid chromatography with hydride generation atomic fluorescence spectroscopy (MD-LC-HGAFS). The decrease of As-III peak response rather than As-V indicated that HSA reacted with As-III but not As-V. The binding plots indicated that the binding between HSA and As-III was in Scatchard pattern when the concentration ratios of As-III to HSA were a parts per thousand currency sign1:1. The strong binding sites (n (1)) were 1.6 and the stability constant (K (1)) was 1.54 x 10(6) M-1. When the concentration ratios of As-III to HSA were > 1:1, the binding was in Plasvento pattern with the stability constant K (2) a parts per thousand... 0 and no specific binding of As-III with HSA. On the contrary, As-V did not show binding with HSA. The results showed that As-III reacted with HSA more readily than As-V, which provides a chemical basis for arsenic toxicity.
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