Abstract
Human oxyhemoglobin reacts with mellitic dianhydride to produce a modified protein which shows a reduced oxygen affinity over a wide pH range, a reduced but significant cooperativity, a reduced Bohr effect and no response to the allosteric effectors: chloride, clofibric acid or inositol hexaphosphate. The amount of crosslinking in the modified hemoglobin is approximately 22% suggesting promise as a blood substitute. Reaction of deoxyhemoglobin with mellitic dianhydride produces a modified protein with reduced response to clofibric acid and a decrease in oxygen affinity in the presence of inositol hexaphosphate.
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Schedule a callMore From: Biomaterials, artificial cells, and immobilization biotechnology : official journal of the International Society for Artificial Cells and Immobilization Biotechnology
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