Characterization of the heme iron in pyridoxylated hemoglobin cross-linked by glutaraldehyde using Mössbauer spectroscopy

The Relationship of Mössbauer Hyperfine Parameters and Structural Variations of Iron Containing Proteins and Model Compounds in Biomedical Research

“…Small variations of Mössbauer hyperfine parameters were also observed for ferritin-like iron in human normal and patient's tissues [10] (Figure 6) and in tissues from normal chicken (see also [11]) and chicken with leukemia ( Figure 7). Small variations of DE Q were found in the study of normal human HbO 2 in solution and in lyophilized form in comparison with those of oxygenated blood substitute based on human hemoglobin modified by pyridoxal-5 0 -phosphate (PLP) and glutaraldehyde (GA) in solution and in lyophilized form [12] ( Figure 8). Some small differences of DE Q were observed for several iron dextran complexes (IDC) which were pharmaceutically important ferritin models [13] (Figure 9).…”

“…T = 87 K. Data were taken from[12]. Differences of quadrupole splitting for IDC and human liver ferritin in lyophilized format 87 K: 0 Y IDC3P; Í Y IDC4P; r Y IDC6P; & Y IDC8P; N Y IDC87; ) Y Ferridextran (Lečiva,Č SSR); Ì Y Imferon (Fisons, UK); q Y Ferritin[13].…”