Gokce, BasakGencer, NahitArslan, OktayKaratas, Mert OlgunAlici, Bulent2024-08-042024-08-0420161475-63661475-6374https://doi.org/10.3109/14756366.2015.1043297https://hdl.handle.net/11616/97295Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. In this study, in vitro effect of some hydroxy and dihydroxy ionic coumarin derivatives (1-20) on purified PON1 activity was investigated. Among these compounds, derivatives 11-20 are water soluble. In investigated compounds, compounds 6 and 13 were found the most active (IC50 = 35 and 34 mu M) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.eninfo:eu-repo/semantics/openAccessCoumarin derivativesin vitro inhibitionparaoxonaseArticle3145345372598229210.3109/14756366.2015.10432972-s2.0-84964618024Q1WOS:000379783200003Q1