The Development of Non-Heme-Oxygen Carriers for Use in Blood Substitutes.
GEORGIA UNIV ATHENS
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In recent years, the structure and oxygen-binding mechanism of the non-heme protein, hemerythrin, have been greatly clarified. These advancements, coupled with rapid developments in cloning technology and increasing demand for safe effective blood substitutes, suggests that investigation of hemerythrin for this purpose should be closely examined. We have recently succeeded in cloning and overexpressing functional hemerythrin. Two general questions are being addressed. First, can hemerythrins be found or engineered by chemical modification or site-directed mutagenesis which find oxygen with P50 greater than 20mm Hg and which are at least as stable as hemoglobin at 37 degrees Celsius. Second, are these proteins retained for at least several hours in the vascular system of a suitable animal host, do they have any vasoconstrictive properties and are they toxic when infused.
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