[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.
Myshkin
A E
AE
D000371:Agglutination / Q000187:drug effects*; D006801:Humans; D007202:Indicators and Reagents; D008628:Mercury / Q000494:pharmacology*; D010108:Oxyhemoglobins / Q000737:chemistry / Q000187:drug effects*; D011487:Protein Conformation / Q000187:drug effects; D012995:Solubility; D012996:Solutions
D007202:Indicators and Reagents; D010108:Oxyhemoglobins; D012996:Solutions; D008628:Mercury
Agregativnaia ustoĭchivost' oksigemoglobina cheloveka v vodnykh sredakh v prisutstvii soedineniĭ rtuti(II).