Serial oxygen equilibrium and kinetic measurements during RBC storage

Objectives: To contribute to the understanding of the biochemical changes associated with the RBC storage lesion. Aim: To investigate changes in O2 equilibrium and on/off kinetic rates during routine cold storage. Background: As RBCs are stored between 1 and 6°C numerous biochemical changes occur wi...

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Published inTransfusion medicine (Oxford, England) Vol. 20; no. 5; pp. 341 - 345
Main Authors Gelderman, M. P., Yazer, M. H., Jia, Y., Wood, F., Alayash, A. I., Vostal, J. G.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.10.2010
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Summary:Objectives: To contribute to the understanding of the biochemical changes associated with the RBC storage lesion. Aim: To investigate changes in O2 equilibrium and on/off kinetic rates during routine cold storage. Background: As RBCs are stored between 1 and 6°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 O2 equilibrium and on/off kinetic rates across the RBC membrane during routine storage. Methods/Materials: The oxygen binding (kon) and offloading (koff) 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 kon increased slightly as the 2,3‐DPG and p50 decreased during storage, whereas the koff remained largely unchanged. The OECs demonstrated the expected increase in O2 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.
Bibliography:ark:/67375/WNG-6Q9F83GB-C
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ArticleID:TME1016
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0958-7578
1365-3148
DOI:10.1111/j.1365-3148.2010.01016.x