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Abstract
The autoxidation rates of hemoglobins crosslinked between the α subunits (α99XLHb A) and between the β subunits (β82XLHb A) were reduced in the presence of catalase and/or superoxide dismutase. In the presence of catalase the rate for α99XLHb A decreased 2.3 fold and for β82XLHb A, 1.9 fold. Superoxide dismutase reduced the rate 1.6 fold for α99XLHb A and 1.8 fold for β82XLHb A. In the presence of both catalase and superoxide dismutase the rate of autoxidation decreased by 3.0 fold in α99XLHb A and 4.0 fold in β82XLHb A. The presence of catalase and superoxide dismutase or both in the crosslinked hemoglobin samples increases the autoxidation half-life of oxyhemoglobins. This suggests that crosslinked hemoglobins to be used as blood substitutes could be protected from oxidation in storage by these enzymes.
