Characterization of binding site of uremic toxins on human serum albumin

Biol Pharm Bull. 1995 Dec;18(12):1755-61. doi: 10.1248/bpb.18.1755.


The interaction of uremic toxins including indole-3-acetic acid (IA), indoxyl sulfate (IS), hippuric acid (HA) and 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF) with human serum albumin (HSA) has been investigated by three methods of fluorescent probe displacement, ultrafiltration and equilibrium dialysis. The binding parameter of CMPF was found to have the strongest affinity (10(7)M-1) among all the uremic toxins studied. Competitive experiment based on the method of Kragh-Hansen suggested that IA, IS and HA bind to site II, whereas CMPF binds to site I. The present limited data indicated that the four uremic toxins caused inhibition to any endo- or exogenous substances on HSA.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Dansyl Compounds / metabolism
  • Furans / metabolism*
  • Hippurates / metabolism*
  • Humans
  • Indoleacetic Acids / metabolism*
  • Indoles / metabolism
  • Propionates / metabolism*
  • Sarcosine / analogs & derivatives
  • Sarcosine / metabolism
  • Serum Albumin / chemistry
  • Serum Albumin / metabolism*
  • Uremia / blood
  • Uremia / chemically induced
  • Warfarin / metabolism


  • Dansyl Compounds
  • Furans
  • Hippurates
  • Indoleacetic Acids
  • Indoles
  • Propionates
  • Serum Albumin
  • dansylsarcosine
  • indoxyl
  • Warfarin
  • indoleacetic acid
  • 3-carboxy-4-methyl-5-propyl-2-furanpropionic acid
  • hippuric acid
  • Sarcosine