Advantage has been taken of the unique affinity of DBBF for hemoglobin to stabilize the T state and crosslink tetrameric hemoglobin. The oxygen affinity has been further decreased by using PLP to produce a chemically unique molecule with a P50 of 32 under physiologic conditions. Furthermore, the modification is specific, requires only reagents that are commercially available or easily synthesized, and can be prepared in large quantities with up to 80% yield. The unique modified hemoglobin was purified by HPLC and the crosslink was found between the beta chains. This derivative, pyridoxalated-fumarate hemoglobin, sustained life in five rats that were 95% exchanged-transfused with the solution. Preliminary in vivo tests support this derivative as a desirable oxygen-transporting resuscitation fluid.
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