ABSTRACT
<p><b>OBJECTIVE</b>To study the effects of salvianolic acid A on content of cytochrome P450,cytochrome b5 and CYP1A2, CYP2E1 activities of rats.</p><p><b>METHOD</b>The rats were randomly divided into two groups and each group contained 5 male rats and 5 female rats. One is control group, another is dosage group. The dosage group was injected salvianolic acid A into a rat tail vein at doses of 20 mg x kg(-1) x d(-1) for 5 days. The control group was injected placebo into a rat tail vein at the same doses as the dosage group. The content of cytochrome P450 and cytochrome b5 of rats were assayed using UV and CYP1A2, CYP2E1 activities were evaluated using probe substrate.</p><p><b>RESULT</b>After salvianolic acid A was injected into rats tail vein for 5 days, the total content of cytochrome P450 and cytochrome b5 and CYP1A2 and CYP2E1 activities have no statistical significance of differences than the control group.</p><p><b>CONCLUSION</b>Salvianolic acid A has no effects on CYP1A2 and CYP2E1 activities, indicating that there is no internation between salvianolic acid A and the drugs metabolized by CYP1A2 or CYP2E1.</p>
Subject(s)
Animals , Female , Male , Rats , Caffeic Acids , Pharmacology , Chromatography, High Pressure Liquid , Cytochrome P-450 CYP1A2 , Metabolism , Cytochrome P-450 CYP2E1 , Metabolism , Cytochrome P-450 Enzyme System , Metabolism , Cytochromes b5 , Metabolism , Lactates , Pharmacology , Microsomes, Liver , Metabolism , Rats, Sprague-DawleyABSTRACT
Objective To study the characteristic of salvianolic acid(SA) binding to bovine serum albumin(BSA) and the structure-performance relationship.Methods The interactions between BSA and four natural SA(SAⅠ,rosmaric acid;SAⅡ,lithosperic acid;SAⅢ,salvianolic acid A;and SAⅣ,salvianolic acid B) were investigated by fluorescence and ultraviolet spectroscopy.Results The intrinsic fluorescence of BSA was quenched by SA via forming SA-BSA complexes and non-radiation energy transfer.The parameters of SA-BSA binding process,such as the static apparent association constant KA,the number of binding site n,the efficiency of energy transfer E,the spatial distance r were obtained,and the thermodynamic constants ?G,?H,and ?S were calculated.Conclusion The results indicate that SAⅢ bounds to BSA mainly through a hydrophobic force and the other three SA-BSA interactions are mainly driven by hydrogen bond and Van der Waals' force.Y,a comprehensive binding parameter constructing from the equation Y=lg (KA?E?n/r),could be used to reflect the interaction extent of SA-BSA system.The Y value changes with the number of free phenolic hydroxyl and molecule volume and decreases in the order of SAⅢ→SAⅣ→SAⅡ→SAⅠ.The results from correlation analysis indicate that it could be possible to estimate SA-BSA binding extent from hydrophobic parameter clogP and topo-polar surface area per unit of molecular weight tPSA/Mr of SA molecule.