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Artificial Cells, Blood Substitutes, and Biotechnology Volume 22, 1994 - Issue 3
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Original Article

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
Pages 517-524 | Published online: 11 Jul 2009
 
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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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