Structure and Function of Lyophilized Human Hemoglobin in Storage at Various Temperatures Over 6 Months
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Date
2023-05
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The Ohio State University
Abstract
The stability of human hemoglobin is of critical importance for applications in therapeutics and tissue engineering. The portability and storage stability of liquid hemoglobin over extended periods of time can pose challenges for the storage and shipment of the materials. Auto-oxidation of oxyhemoglobin to methemoglobin in storage reduces the concentration of ferrous hemoglobin available for oxygen transport. This study aims to address these challenges and determine the optimal storage temperature of lyophilized human hemoglobin by evaluating its' structural and functional properties in storage over 6 months. Following a comprehensive analysis of lyophilized human hemoglobin's structural and functional properties, we found that storage under refrigerated conditions – 4 °C, -20 °C, and -80 °C – resulted in a significant reduction in methemoglobin composition compared to storage at room temperature. Additionally, the refrigerated carboxyhemoglobin samples retained their oxygen equilibrium properties and underwent minimal changes in their tetrameric structure. Therefore, we demonstrate a viable strategy for the storage of hemoglobin in the carboxy form, which preserves its long-term structural and functional properties. Overall, we determined that lyophilized carboxyhemoglobin is an excellent candidate to preserve the structural and functional capability of the protein under refrigerated conditions.
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Keywords
Hemoglobin, Storage, Lyophilization, Structure, Function