title: Serum albumin--a non-saturable carrier.
abstract: The shape of binding isotherms for sixteen ligands to human serum albumin showed no signs of approaching saturation at high ligand concentrations. It is suggested that ligand binding to serum albumin is essentially different from saturable binding of substrates to enzymes, of oxygen to haemoglobin, etc. Binding to serum albumin appears to be non-saturable.
mesh_terms: D001663:Bilirubin / Q000378:metabolism; D003956:Dialysis; D006801:Humans; D008024:Ligands; D004364:Pharmaceutical Preparations / Q000097:blood*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D008024:Ligands; D004364:Pharmaceutical Preparations; D012709:Serum Albumin; D001663:Bilirubin