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Enzymatic protection from autoxidation for crosslinked hemoglobins.

作者信息

Yang T, Olsen K W

机构信息

Department of Chemistry, Loyola University of Chicago, IL 60626.

出版信息

Artif Cells Blood Substit Immobil Biotechnol. 1994;22(3):709-17. doi: 10.3109/10731199409117902.

DOI:10.3109/10731199409117902
PMID:7994392
Abstract

The autoxidation rates of hemoglobins crosslinked between the alpha subunits (alpha 99XLHb A) and between the beta subunits (beta 82XLHb A) were reduced in the presence of catalase and/or superoxide dismutase. In the presence of catalase the rate for alpha 99XLHb A decreased 2.3 fold and for beta 82XLHb A, 1.9 fold. Superoxide dismutase reduced the rate 1.6 fold for alpha 99XLHb A and 1.8 fold for beta 82XLHb A. In the presence of both catalase and superoxide dismutase the rate of autoxidation decreased by 3.0 fold in alpha 99XLHb A and 4.0 fold in beta 82XLHb 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.

摘要

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