Changes in 2,3-DPG Content and Oxygen Affinity in Erythrocytes Stored at 4°C

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Abstract
The 2,3-DPG [2,3-diphosphoglycerate] content of [human] red blood cells [RBC] increased within the first 24 h when fresh erythrocytes or whole blood were stored at 4.degree. C. This phenomenon was strongly pH dependent. The temporary increase in 2,3-DPG was scarcely observed below pH 7.4 or above pH 7.8. With whole blood, the increase was observed in CPD [citrate-phosphate-dextrose] blood but not in ACD [acid-citrate-dextrose] blood. Similar results were obtained with RBC suspended in saline, when its pH was adjusted to approximately 7.6. Plasma proteins were not essential for the increase in 2,3-DPG content. Extracellular O2 levels were continually measured in RBC suspensions to check the changes in O2 affinity of Hb without damaging the cells. Extracellular O2 levels and 2,3-DPG contents were simultaneously increased by keeping fresh RBC at 4.degree. C. Inhibition of glycolysis with NaF and monoiodoacetic acid indicated that the in vivo steady state of glycolysis in RBC might be altered by chilling to make the rate of 2,3-DPG synthesis faster than that of 2,3-DPG decomposition.