The aggregative stability of human oxyhemoglobin in aqueous media in the presence of mercury(II) compounds]

An analytical review of studies on human oxyhemoglobin coagulation has been performed by the author jointly with V. S. Koniaeva and L. D. Bogdanova within a period from 1985 to 1990. It was shown that the oxyhemoglobin coagulation modified by mercurials proceeded without any essential alteration of native protein conformation. A hypothesis is discussed that the oxyhemoglobin coagulation results from the primary polyaggregation of dimer fragments and that hydrophobic sites which provide for dimer-to-dimer contacts in native tetrameric oxyhemoglobin, participate in this process.