[Gamma-resonance spectrometry study of the nonequilibrium states of hemoglobin].
Reduction of frozen water-glycerol solutions of methemoglobin by thermolysed electrons at 77 degrees K has been studied by Mossbauer spectroscopy. The formation of nonequilibrium hemoglobin states with two slightly different low-spin ferroforms was observed. The latter is explained by the presence of two ferroforms in initial methemoglobin. There was observed relaxation of the conformation - nonequilibrium states up to equilibrium hemoglobin with high-spin Fe(II) at the sample disfreezing.
D003037:Cobalt Radioisotopes; D004583:Electrons; D005292:Ferricyanides; D007501:Iron; D008706:Methemoglobin / Q000528:radiation effects; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013051:Spectrometry, Gamma; D013696:Temperature
D003037:Cobalt Radioisotopes; D005292:Ferricyanides; D008706:Methemoglobin; D007501:Iron; C028033:potassium ferricyanide
Issledovanie neravnovesnykh sostoianiĭ gemoglobina metodom gamma-rezonansnoĭ spektrometrii.