[Parameters of interaction of nitrophenols with different chemical structure with albumin, and their toxicity].

Chemical structure of a series of nitrophenols and their derivatives was studied in relation to their toxicity and complex-formation ability (association constant, amount of binding sites) with human blood serum albumin. Five compounds were studied using equilibrium dialysis and spectrofluorimetry. The nitrophenols, containing a hydrocarbon radical, exhibited distinctly higher affinity to albumin; substitution of one or two nitrogroups by aminogroups led to complete loss of the affinity to the protein. Dependence of acute toxicity on association constants of the complexes is discussed.