Abstract
The incubation of stored blood in a mixture of inosine, pyruvate, glucose, and phosphate restores the O2 affinity of hemoglobin to physiologic levels, as measured by the configuration of the dissociation curve and the P50. This regeneration of normal hemoglobin function not only is consistent for samples anticoagulated with EDTA and stored eight days at 4 C but also is demonstrable for at least 19 days of 4 C storage of EDTA-anticoagulated whole blood. This regeneration procedure is simple to perform and makes it possible to measure reliably O2 affinity in blood samples transmitted by mail.
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