Serial oxygen equilibrium and kinetic measurements during RBC storage

Blood storage at low temperatures leads to gradual deterioration of red blood cells (RBCs), known as the storage lesion. This process involves biochemical and structural changes that may affect RBC function. Prior research has shown that cold storage alters hemoglobin properties, including oxygen binding and release. However, the specific dynamics of oxygen equilibrium and kinetic rates during storage remain unclear. No prior work had resolved how these parameters evolve over time in stored RBCs. This gap motivated the current investigation into oxygen binding and unbinding rates. Understanding these changes could clarify how stored RBCs maintain their function. The study aimed to address this uncertainty by measuring oxygen interaction rates during storage. These findings may help refine storage protocols and transfusion practices.

This study aimed to measure oxygen binding and unloading rates in stored RBCs to better understand the storage lesion. Researchers sought to determine how oxygen equilibrium and kinetic rates change during cold storage. The specific problem addressed is the lack of data on oxygen interaction dynamics in stored RBCs. The motivation stems from the need to preserve RBC function during storage. The study focused on oxygen binding (k(on)) and unloading (k(off)) constants. These parameters were measured in fresh and stored RBCs at weekly intervals. The goal was to assess how these values evolve during storage. The results could inform transfusion medicine about RBC viability.

The study used fresh and AS-5-preserved RBCs stored at 1–6°C. Oxygen binding (k(on)) and unloading (k(off)) constants were measured weekly. Oxygen equilibrium curves (OECs) were generated to assess oxygen affinity. 2,3-Diphosphoglycerate (2,3-DPG) levels and p50 values were also measured. The Hill number (n) was calculated to evaluate cooperativity. These measurements were taken at multiple time points over 42 days. The experimental design allowed tracking of changes in oxygen interaction rates. The data were analyzed to determine trends in oxygen binding and release.

Oxygen binding (k(on)) increased slightly during storage as 2,3-DPG and p50 decreased. Oxygen unloading (k(off)) remained largely unchanged over the storage period. Oxygen equilibrium curves showed increased oxygen affinity with storage. The Hill number (n) did not change significantly during storage. These findings suggest that RBCs maintain their oxygen interaction capacity. The observed changes in k(on) and 2,3-DPG suggest a shift in oxygen binding dynamics. Despite biochemical changes, functional oxygen interactions were preserved. The results indicate that RBCs retain key functional properties during storage.

The study found that RBCs maintain their oxygen interaction capacity during cold storage. Oxygen binding (k(on)) increased slightly while unloading (k(off)) remained stable. Oxygen affinity increased, but cooperativity (Hill number) was unchanged. These findings suggest that RBCs retain functional oxygen properties. The results support the idea that stored RBCs remain viable for transfusion. The observed changes do not appear to compromise oxygen delivery. The study contributes to understanding the storage lesion. These findings may help guide blood storage and transfusion protocols.