Preparation and characterization of dimeric bovine hemoglobin tetramers.
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.
Hu
Tao
T
National Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
Li
Dongxia
D
Su
Zhiguo
Z
D000818:Animals; D002417:Cattle; D002712:Chlorides / Q000494:pharmacology; D019281:Dimerization; D006454:Hemoglobins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007477:Ions / Q000494:pharmacology; D010100:Oxygen / Q000378:metabolism; D020836:Protein Structure, Quaternary / Q000187:drug effects
D002712:Chlorides; D006454:Hemoglobins; D007477:Ions; D010100:Oxygen