Hemoglobin oxidation

Quercetin and rutin suppressed photosensitized hemolysis of human erythrocytes with ho values equal to 40 p.mol l-1 and 150 jjlmt>I I 1, respectively [139]. Suppression of photohemolysis was accompanied by inhibition of lipid peroxidation. Morin inhibited oxygen radical-mediated damage induced by superoxide or peroxyl radicals to the human cells in the cardiovascular system, erythrocytes, ventricular myocytes, and saphenous vein endothelial cells [140]. Rutin protected against hemoglobin oxidation inside erythrocytes stimulated by prooxidant primaquine [141],... 

Jarolim, P., Lahav, M., Liu, S. C., and Palek, J. (1990). Effect of hemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins Correlation with a release of hemin. Blood 76, 2125-2131. 

Potter WT, Rong S, Griffith J, et al. 1991. Phosphine-mediated Heinz body formation and hemoglobin oxidation in human erythrocytes. Toxicol Lett 57 37-45. 

Lips, V. Celeddn, G. Escobar, J. Lissi, E.A. Thiol-induced hemoglobin oxidation. Redox Report 1996, 2 (3), 205-212. 

Fig. 9 The effect of residual water on the stability of freeze-dried proteins. Circles = human growth hormone deamidation and oxidation at 25° C, %/month squares = aggregation of human serum albumin at 50°C, %/day triangles = hemoglobin oxidation at 23° C in a sucrose formulation, %/year (From Ref - - l)...

Tarburton JP, Metcalf WK. Kinetics of amyl nitrite-induced hemoglobin oxidation in cord and adult blood. Toxicology 1985 36(1) 15-21. 

The intramolecular reaction mechanism for hemoglobin oxidation proposed by Lemberg and Legge in which only the intermediate Hb4(02)2 undergoes a reaction has been discussed above. The fact that the mechanism cannot account for the oxidation at high oxygen pressures makes it... 

Human hemoglobin oxidation with Fe(lll)-heme formation as a result of the vanadyl ion effect was observed using Mossbauer spectroscopy [ 105]. Partial oxidation of rat hemoglobin after 70 days of rats feeding with cerium chloride was detected by Mossbauer spectroscopy [106]. An attempt to study hemoglobin from patients with diabetes was done in Ref. 107. However, poor statistical rates, a low signal-to-noise ratio, and a low velocity resolution in these studies did not permit the authors to extract more detailed and exact information. 

Some studies have suggested that the sulfhydryl groups of glutathione (GSH) prevented hemoglobin oxidation and in this maimer are essential for the maintenance of intact erythrocyte structure. In an in vitro study, a decrease in reduced GSH concentration in human RBCs was found to correlate with the hemolytic action of arsine (Rael et al., 2000). Blair et al. (1990) recorded a 60% decrease in reduced GSH level in erythrocytes exposed to arsine in vitro. However, Hatlelid et al. (1995) showed that the depletion of reduced GSH in RBCs in dogs neither preceded nor coincided with hemolysis. 

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