Abstract
Dimeric bovine hemoglobin (Hb) tetramers were prepared by a one-step solid phase adsorption method. Briefly, Hb was absorbed by the solid phase, Q Sepharose Fast Flow media, followed by reaction with the glutaraldehyde and elution procedure. Then, dimeric bovine Hb tetramers were formed and purified from Hb tetramers by anion-exchange chromatography based on Protein-Pak DEAE 8HR. The dimeric Hb tetramer showed a P50 value of 15.9 mm Hg, oxygen transporting efficiency of 14.2%, and Hill coefficient of 1.72. The number of Bohr protons released for dimeric Hb tetramers was 0.59 H/tetramer, which was 39% of that of native bovine Hb. The number of chloride ions released on oxygenation was 0.60/tetramer for dimeric Hb tetramers, which was 46% of that of native bovine Hb.
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Hu, T., Li, D. & Su, Z. Preparation and Characterization of Dimeric Bovine Hemoglobin Tetramers. J Protein Chem 22, 411–416 (2003). https://doi.org/10.1023/B:JOPC.0000005455.94103.b8
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DOI: https://doi.org/10.1023/B:JOPC.0000005455.94103.b8