Modification of hemoglobin upon covalent coupling to dextran: enhanced stability against acid denaturation and reduced affinity for haptoglobin

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Abstract
Alkylation of human Hb by bromoacetylaminoethylamino-substituted dextran gave rise to a covalent dextran-Hb complex with enhanced stability against acid denaturation and reduced affinity for binding to haptoglobin, compared with free Hb. These effects increased with increasing size of the dextran moiety and were not elicited by either free dextran or alkylation of Hb by iodoacetamide. These observations are consistent with an inhibition by covalently attached dextran of the binding of .beta.-subunit of Hb to haptoglobin.