In vitro binding of 14C-labeled acidic compounds to serum albumin and their tissue distribution in the rat.
The acidic compounds, such as phenoxyacetic acids, substituted benzoic acids, or acetylsalicylic acid, were found to bind to bovine serum albumin (BSA). Among phenoxyacetic acids, the binding affinity to BSA was highest for 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), which was approximately 4-, 24-, and 160-fold greater than those for 2,4-dichlorophenoxyacetic acid (2,4-D), o-chlorophenoxyacetic acid (CPA), and phenoxyacetic acid (PAA), respectively. There were two bound to serum albumins of other mammalian species. The binding affinity varied among species and also depended on the chemicals. However, the order of binding affinity in the albumin of each species remained the same as observed in BSA with few exceptions. Blood/tissue ratios of 14C from rats dosed with these 14C-labeled acids were highly correlated with the logarithm of the binding affinity constantsaffinity constants.
D000818:Animals; D001241:Aspirin / Q000097:blood; D002264:Carboxylic Acids / Q000097:blood*; D002417:Cattle; D002723:Chlorobenzoates / Q000097:blood; D006168:Guinea Pigs; D006736:Horses; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D011817:Rabbits; D051381:Rats; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012756:Sheep; D013552:Swine; D014018:Tissue Distribution
D002264:Carboxylic Acids; D002723:Chlorobenzoates; D012709:Serum Albumin; C024798:Amiben; D012710:Serum Albumin, Bovine; D001241:Aspirin