title: [Oxygen-binding properties of human hemoglobin solutions UV-irradiated in the presence of iodoacetamide].
abstract: Changes of oxygen-binding properties of human hemoglobin solutions modified by the different concentrations of iodoacetamide and by this chemical agent together with UV-light in doses 151 and 755 J/m2 has been studied by means of spectroscopy. It has been shown that addition of iodoacetamide to native hemoglobin solution (12:1) results in increase of the oxygen affinity and breach of the hem-hem interaction of hemoprotein. It has been ascertained that influence of UV-radiation on hemoglobin displays in photodissociation of the tetramers to protomers.
authors.forename: G A
authors.initials: GA
authors.lastname: Vashanov
authors.forename: V G
authors.initials: VG
authors.lastname: Artiukhov
authors.forename: M V
authors.initials: MV
authors.lastname: Bavykina
mesh_terms: D000328:Adult; D001798:Blood Proteins / Q000032:analysis; D006801:Humans; D066298:In Vitro Techniques; D007460:Iodoacetamide / Q000494:pharmacology*; D010108:Oxyhemoglobins / Q000187:drug effects* / Q000528:radiation effects*; D011829:Radiation Dosage; D012996:Solutions; D013057:Spectrum Analysis; D014466:Ultraviolet Rays
chemical_list: D001798:Blood Proteins; D010108:Oxyhemoglobins; D012996:Solutions; D007460:Iodoacetamide
vernacular_title: Kislorodsviazyvaiushchie svoĭstva rastvorov gemoglobina cheloveka, UF-obluchennykh v prisutstvii ĭodatsetamida.