| Autor: |
Tao Hu, Dongxia Li, Zhiguo Su |
| Předmět: |
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| Zdroj: |
Journal of Protein Chemistry; Jul2003, Vol. 22 Issue 5, p411-416, 6p, 1 Black and White Photograph, 9 Graphs |
| Abstrakt: |
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 P[sub 50] 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. KEY WORDS: Dimeric hemoglobin tetramers; hemoglobin; glutaraldehyde; oxygen therapeutics. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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