Preparation and oxygen binding properties of soluble covalent hemoglobin-dextran conjugates |
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Authors: | F. Bonneaux P. Labrude E. Dellacherie |
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Affiliation: | (1) Laboratoire de Chimie-Physique Macromoléculaire-ERA no 23 Ensic, 1, rue Grandville, F-54042 Nancy Cedex, (France);(2) Centre Régional de Transfusion Sanguine, F-54500 Vanduvre-les-Nancy, (France) |
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Abstract: | Summary Stroma-free hemoglobin solutions present some drawbacks when used as blood substitutes, essentially because the hemoprotein has a low vascular retention, due to its small hydrodynamic volume. Covalent coupling of the protein with dextran derivatives artificially increases its size and affords polymeric conjugates whose oxygen-binding properties (Barcroft's curve, Hill coefficient) depend on the molecular weight.The authors wish to thank Prof. J. Neel and Prof. C. Vigneron for useful discussions and criticism. |
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