[Molecular mechanisms of interaction between blood serum albumin and dinitroorthocresol].

Interactions of dinitroortocresol with human blood serum albumin were studied using equilibrium dialysis, spectrofluorimetry and polarography. Two classes of binding sites were found in the protein molecule: high-affinity site, binding 4 molecules of cresol and a low-affinity site, binding up to 12 molecules. Binding of dinitroortocresol occurred simultaneously with alteration in the albumin molecule conformation.