Characterization of beta-hydroxy-beta-methylglutaryl coenzyme A reductase inhibitor from Pueraria thunbergiana

J Agric Food Chem. 2005 Jul 27;53(15):5882-8. doi: 10.1021/jf0505978.

Abstract

This study describes the extraction and characterization of an inhibitor for beta-hydroxy-beta-methylglutaryl (HMG) coenzyme A (CoA) reductase from Pueraria thunbergiana. The maximum HMG-CoA reductase inhibitory activity (IC(50) = 79 microg) was obtained when P. thunbergiana was extracted with 70% ethanol at 30 degrees C for 12 h. After purification of the HMG-CoA reductase inhibitor by means of systematic solvent extraction, silica gel column chromatography, and HPLC, an active fraction with an IC(50) of 0.9 microg (4.25 microM) and a yield of 1.3% was obtained. The purified HMG-CoA reductase inhibitor was identified as daidzein (C(15)H(10)O(4); molecular mass, 254 Da).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chlorocebus aethiops
  • Cricetinae
  • Hydroxymethylglutaryl CoA Reductases / metabolism
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors / isolation & purification*
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors / pharmacology*
  • Hypolipidemic Agents / pharmacology
  • Mesocricetus
  • Pueraria / chemistry*
  • Vero Cells

Substances

  • Hydroxymethylglutaryl-CoA Reductase Inhibitors
  • Hypolipidemic Agents
  • Hydroxymethylglutaryl CoA Reductases