[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.
D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D005260:Female; D006801:Humans; D007928:Lethal Dose 50; D008297:Male; D009596:Nitrophenols / Q000633:toxicity; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin; D013329:Structure-Activity Relationship
D009596:Nitrophenols; D012709:Serum Albumin
Parametry vzaimodeĭstviia nitrofenolov razlichnogo khimicheskogo stroeniia s al'buminom i ikh toksichnost'.