Abstract
The phenoxyalkanoix acids are bound to bovine serum albumin at a single site of high affinity, where the interaction is most importantly influenced by strong hydrophobic bonding, with ionic bonding being of lesser importance, and also at several sites of lower affinity. The hydrophobic binding site has almost equal affinity for the phenoxy groups of 2,4-dichlorophenoxyacetic acid, 4-(2,4-dichlorophenoxy)butyric acid and 2-(2,4,5-trichlorophenoxy)propionic acid and greater affinity for the phenoxy group of 2,4,5-trichlorophenoxyacetic acid. The properties of the high affinity binding site bear some resemblance to the properties of the amino acid sequence adjoining the tryptophan residue of human serum albumin, and evidence is presented for the presence of tryptophan at the high affinity binding site of bovine serum albumin.
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