Protein Bindings. VI. Binding of Phenols to Bovine Serum Albumin

Abstract

Binding constant, K, for 23 phenols with bovine serum albumin was evaluated spectrophotometrically utilizing the albumin-induced metachromasia of 2-(4'-hydroxyphenylazo)-benzoic acid. In the binding, electrostatic force seems dominant but hydrophobic binding may not be negligible with 2, 4-dichlorophenol and 2, 4, 5-trichlorophenol. The values of log K generally correlated with pK_a, in vitro bacteriostatic activity against Staphylococcus aureus 209 P, action of uncoupling oxidative phosphorylation at mitochondria, and π-electron-density for the oxygen-atom of phenolic hydroxy group of phenols,