Hemoglobin function in stored blood.

H F Bunn; M H May; W F Kocholaty; C E Shields

doi:10.1172/jci105987

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Hemoglobin function in stored blood.

H F Bunn·M H May·W F Kocholaty·C E Shields

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Abstract

Serial oxygen dissociation curves were performed on blood units preserved in acid-citrate-dextrose (ACD), ACD-adenine, and ACD-adenine-inosine. Dividing blood from a single donor into two or more bags allowed direct comparison between preservatives. During the 1st wk of storage in ACD, a progressive increase in oxygen affinity was observed. Thereafter, little further change was noted. Oxygen affinity increased even more rapidly during initial storage in ACD-adenine. However, with the inclusion of inosine as a preservative, oxygen affinity remained unaltered during the first 2 wk. Increases in oxygen affinity correlated well with falling levels of red cell 2,3-diphosphoglycerate (2,3-DPG) during storage. No significant changes in glutathione, reduced form (GSH), or A3 (A(I)) hemoglobin levels were noted during the first 3 wk of storage. No significant accumulation of ferrihemoglobin was detected. When blood stored 20 days in ACD or ACD-adenine was incubated with inosine for 60 min at 37 degrees C, 2,3-DPG and adenosine triphosphate (ATP) were resynthesized, and oxygen affinity was decreased. The distribution of 2,3-DPG in fresh and stored red cells appeared to influence experimental values for Hill's n, a measure of heme-heme interaction.

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Adenine Adenosine Triphosphate Blood Preservation Citrates Glucose Glutathione Glycerophosphates Hemoglobins Humans Hydrogen-Ion Concentration In Vitro Techniques Nucleosides Oxygen Oxygen Consumption Journal Article

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H F Bunn, M H May, W F Kocholaty, C E Shields. 1969. Hemoglobin function in stored blood.. https://doi.org/10.1172/jci105987

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