Effects of an oxidative stress on human hemoglobin: a multiwavelength visible spectrometry study

• Published in: Biomedicine & pharmacotherapy Vol. 59; no. 5; pp. 230 - 232
• Main Authors: Lenfant, François, Bureau, Alain, Lahet, Jean-Jacques, Bouyer, Frédéric, Chaillot, Bernard, Freysz, Marc
• Format: Journal Article
• Language: English
• Published: Paris Elsevier SAS 01.06.2005; Elsevier
• Subjects: AAPH; Adult; Amidines - toxicity; Biological and medical sciences; Chemical Sciences; Erythrocyte; Erythrocytes - drug effects; Erythrocytes - metabolism; Hemoglobins - metabolism; Hemolysis; Hemolysis - drug effects; Humans; In Vitro Techniques; Life Sciences; Medical sciences; Oxidants - toxicity; Oxidative Stress - drug effects; Pharmaceutical sciences; Pharmacology; Pharmacology. Drug treatments; Potassium - metabolism; Spectrometry; Spectrum Analysis - methods; Hemolysis; Erythrocyte; Spectrometry; AAPH; Human; Oxidative stress; Blood cell; Red blood cell; Hemoglobin
• ISSN: 0753-3322; 1950-6007
• DOI: 10.1016/j.biopha.2004.06.007

This study was carried out to investigate hemoglobin behavior and the role of cell membrane during oxidative stress of human red blood cells induced by a water-soluble radical initiator, 2,2′-azobis(amidino-propane) hydrochloride (AAPH) and compare the observed data to the one obtained with purified human haemoglobin solution. The different forms of hemoglobin were identified and quantified by multiwavelength visible spectrometry using multiple linear regression analysis. Hemolysis was quantified by the Drabkin method. Oxidative stress on purified hemoglobin solutions induced an early formation of Hb +. In intact erythrocytes, no modified form of haemoglobin was found. Only the hemoglobin released by hemolysis in the extracellular medium was notified in the same way as purified haemoglobin. Thus, the cell membrane appears to protect intraerythrocytic hemoglobin toward an extracellular oxidative stress. Oxidative stress-induced by hemolysis does not seem to be due to changes in intraerythrocytic hemoglobin forms.