Enhanced Oxidation of Bis(3,5-Dibromosalicyl) Fumarate α-α Cross Unked Hemoglobin by Free Radicals Generated by Xanthine/Xanthine Oxidase

M. Samaja Department of Biomedical Science and Technology Scientific Institute San Raffaele, University of Milano, via Olgettina 60, 20132, Milano, ITALY

R. Motterlini Department of Biomedical Science and Technology Scientific Institute San Raffaele, University of Milano, via Olgettina 60, 20132, Milano, ITALY

E. Rovida Department of Biomedical Science and Technology Scientific Institute San Raffaele, University of Milano, via Olgettina 60, 20132, Milano, ITALY

Abstract

The xanthine/xanthine oxidase reaction produces reproducible amounts of oxygen-derived free radicals that oxidize human oxyhemoglobin (Hb). We monitored the kinetics of the oxidation of stripped Hb (sHb), purified HbA₀ and α-α cross-linked Hb (HbXL99α) at [Hb] in the 5 to 150 μM (heme) range. For increasing [Hb], the oxidation halftime (t1/2) increased for all Hbs, but t1/2 was always less for HbXL99α than for HbA₀ and sHb. Such feature was attributed to the lower affinity for O₂ of HbXL99α and may represent a serious problem for use of this Hb as blood substitute.

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Enhanced Oxidation of Bis(3,5-Dibromosalicyl) Fumarate α-α Cross Unked Hemoglobin by Free Radicals Generated by Xanthine/Xanthine Oxidase

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Enhanced Oxidation of Bis(3,5-Dibromosalicyl) Fumarate α-α Cross Unked Hemoglobin by Free Radicals Generated by Xanthine/Xanthine Oxidase

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