Changes in 2,3-DPG content and oxygen affinity in erythrocytes stored at 4 degrees C.

The 2,3-DPG content of red blood cells increased within the first 24 h when fresh erythrocytes or whole blood were stored 4 degrees 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. In the case of whole blood, the increase was observed in CPD blood out not in ACD blood. Similar results were obtained with erythrocytes 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 oxygen levels were continually measured in erythrocytes suspensions in order to check the changes in oxygen affinity of hemoglobin without damaging the cells. Both extracellular oxygen levels and 2,3-DPG contents were simultaneously increased by keeping fresh erythrocytes at 4 degrees C. Inhibition of glycolysis with sodium fluoride and monoidoacetic acid indicated that the in vivo steady state of glycosis in erythrocytes might be altered by chilling to make the rate of 2,3-DPG synthesis faster than that of 2,3-DPG decomposition.