PMID: 6161683Sep 1, 1980Paper

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

Canadian Journal of Biochemistry
S C Tam, J T Wong

Abstract

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

Citations

Oct 8, 1999·Il Farmaco·F M Veronese, M Morpurgo
Jan 31, 2009·Artificial Organs·Jan SimoniJohn F Moeller
Sep 9, 2017·Artificial Cells, Nanomedicine, and Biotechnology·Jun ZhangHong Zhou
Mar 1, 1983·Vox Sanguinis·F DeVenuto
Jan 1, 1992·Biomaterials, Artificial Cells, and Immobilization Biotechnology : Official Journal of the International Society for Artificial Cells and Immobilization Biotechnology·Y Iwashita

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