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Preservation of metabolic activity in lyophilized human erythrocytes.
Author(s) -
Raymond P. Goodrich,
Samuel Sowemimo-Coker,
Charles R. Zerez,
Kouichi Tanaka
Publication year - 1992
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.3.967
Subject(s) - pentose phosphate pathway , biochemistry , triosephosphate isomerase , enzyme , chemistry , pyruvate kinase , glycolysis , oxidative phosphorylation , metabolism , adenine nucleotide , phosphotransferase , nucleotide , gene
Normal human erythrocytes (RBC) were freeze-dried under conditions that caused minimal modification in normal RBC metabolic activities. Because of the known effects of long-term storage on metabolic activities, we studied the effects of our lyophilization process on RBC metabolism. Of all the metabolic enzymes studied, only triosephosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1), enolase (2-phospho-D-glyceratehydro-lyase, EC 4.2.1.11), and pyruvate kinase (ATP:pyruvate O2-phosphotransferase, EC 2.7.1.40) were decreased when compared with fresh control nonlyophilized RBC. The activities of these enzymes did not differ significantly from those of blood bank RBC. Concentrations of high-energy intermediates, ATP, and 2,3-diphosphoglycerate, along with lactate and ATP production were decreased in lyophilized RBC. No enzymes of the pentose phosphate shunt were altered during lyophilization. In addition, our data show that lyophilized RBC possess an intact capacity to (i) synthesize adenine nucleotides and (ii) reduce MetHb to Hb and, thus, maintain the Hb in a functional physiologic state similar to fresh nonlyophilized RBC. The present study demonstrates the possibility of lyophilizing RBC in a manner that maintains normal metabolic and enzymatic function upon rehydration.

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