Serial oxygen equilibrium and kinetic measurements during RBC storage

被引:26
作者
Gelderman, M. P. [3 ]
Yazer, M. H. [1 ,2 ]
Jia, Y. [4 ]
Wood, F. [4 ]
Alayash, A. I. [4 ]
Vostal, J. G. [3 ]
机构
[1] Univ Pittsburgh, Inst Transfus Med, Pittsburgh, PA 15213 USA
[2] Univ Pittsburgh, Dept Pathol, Pittsburgh, PA 15213 USA
[3] US FDA, Lab Cellular Hematol, Div Hematol, Ctr Biol Evaluat & Res, Rockville, MD 20857 USA
[4] US FDA, Lab Biochem & Vasc Biol, Div Hematol, Ctr Biol Evaluat & Res, Rockville, MD 20857 USA
关键词
2,3-DPG; haemoglobin; oxygen dissociation; rate constants; red blood cell; storage lesion; STORED-BLOOD; NITRIC-OXIDE; HEMOGLOBIN;
D O I
10.1111/j.1365-3148.2010.01016.x
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Objectives: To contribute to the understanding of the biochemical changes associated with the RBC storage lesion. Aim: To investigate changes in O-2 equilibrium and on/off kinetic rates during routine cold storage. Background: As RBCs are stored between 1 and 6 degrees C numerous biochemical changes occur within the RBCs, including changes in the properties of the haemoglobin itself. This study serially analysed for the first time the O-2 equilibrium and on/off kinetic rates across the RBC membrane during routine storage. Methods/Materials: The oxygen binding (k(on)) and offloading (k(off)) constants were measured in fresh RBCs and then in AS-5-preserved RBCs at weekly intervals, along with oxygen equilibrium curves (OECs), 2,3-Diphosphoglycerate (2,3-DPG), p50 and the Hill number (n). Results: The k(on) increased slightly as the 2,3-DPG and p50 decreased during storage, whereas the k(off) remained largely unchanged. The OECs demonstrated the expected increase in O-2 affinity, whereas the Hill number was unchanged during storage. Conclusion: In spite of the biochemical, structural and functional changes associated with the storage of RBCs, their in vitro interactions with oxygen were largely preserved through 42 days of storage.
引用
收藏
页码:341 / 345
页数:5
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