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2000 (1)
1Author    M. I. Oshtrakh, O. B. Milder, V. A. Semionkin, A. L. Berkovsky, M. A. Azhigirova, E. P. VyazovaRequires cookie*
 Title    Variation of Quadrupole Splitting in Modified Oxyhemoglobin: A Mössbauer Effect Study  
 Abstract    Human adult hemoglobin modified by both pyridoxal-5'-phosphate and glutaraldehyde in the oxy-form was studied by Mössbauer spectroscopy. Mössbauer spectra were measured at 87 and 295 K (hemoglobin in lyophilized form) and at 87 K (hemoglobin in frozen solution). The values of the quadrupole splitting for modified oxyhemoglobin were found to be lower then those of oxyhemoglobin without modifications in lyophilized form and frozen solution, respectively. The Mössbauer spectra of modified oxyhemoglobin were also analyzed in terms of the heme iron inequivalence in a-and /3-subunits of the tetramer. Differences of the tendencies of temperature dependencies of quadrupole splitting for modified and non-modified oxyhemoglobin in lyophilized form were shown. 
  Reference    Z. Naturforsch. 55a, 193—198 (2000); received September 11 1999 
  Published    2000 
  Keywords    Hemoglobin, Mössbauer Spectroscopy, Quadrupole Spitting 
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 TEI-XML for    default:Reihe_A/55/ZNA-2000-55a-0193.pdf 
 Identifier    ZNA-2000-55a-0193 
 Volume    55