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Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Characterization of the heme iron in pyridoxylated hemoglobin cross-linked by glutaraldehyde using Mössbauer
M I Oshtrakh1, O B Milder, V A Semionkin
1Division of Applied Biophysics, Faculty of Physical Techniques and Devices for Quality Control, Ural State Technical University, 620002, Ekaterinburg, Russia. oshtrakh@soek.erl.e-burg.ru
Abstract:
The heme iron in human adult hemoglobin modified by both pyridoxal-5'-phosphate and glutaraldehyde was characterized by Mössbauer spectroscopy and compared with non-modified hemoglobin. Mössbauer spectra of the samples were measured at 87 and 295 K (1yophilized form) and at 87 K (frozen solution). The values of quadrupole splitting for the oxy-form of modified hemoglobin were found to be lower than those of the oxy-form of hemoglobin without modifications in lyophilized form and frozen solution, respectively. On the other hand, the values of quadrupole splitting for the deoxy-form of modified and non-modified hemoglobins in frozen solution were the same. The Mössbauer spectra of the oxy-form of modified hemoglobin were also analyzed in terms of the heme iron non-equivalence in alpha- and beta-subunits of tetramer. The differences of the tendencies of temperature dependencies of quadrupole splitting for the oxy-form of modified and non-modified hemoglobins in lyophilized form were shown. These results indicated that the heme iron electronic structure and stereochemistry were changed in the oxy-form of pyridoxylated hemoglobin cross-linked by glutaraldehyde.
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