Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane

被引:182
作者
Fan, CH
Wang, HY
Sun, S
Zhu, DX
Wagner, G
Li, GX
机构
[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA
[2] Nanjing Univ, Dept Biochem, Nanjing 210093, Peoples R China
[3] Nanjing Univ, Natl Lab Pharmaceut Biotechnol, Nanjing 210093, Peoples R China
[4] Nanjing Univ, Dept Comp Sci, Nanjing 210093, Peoples R China
关键词
D O I
10.1021/ac001397s
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Hemoglobin can exhibit a direct electron-transfer reaction after being entrapped in a SP Sephadex membrane. A pair of stable and well-defined redox waves are obtained at a hemoglobin-SP sephadex modified pyrolytic graphite electrode. The anodic and cathodic peak potentials are located at -0.244 and -0.336 V (vs SCE), respectively. On the other hand, the peroxidase activity of the protein in the membrane is also greatly enhanced. The apparent Michaelis-Menten constant is calculated to be 1.9 mM, which shows a large catalytic activity of hemoglobin in the SP Sephadex membrane toward hydrogen peroxide (H2O2) According to the direct electron-transfer property and enhanced peroxidase activity of Hb in the membrane, a Hb/SP Sephadex membrane-based H2O2 biosensor is prepared, with a linear range similar to5.0 x 10(-6) to 1.6 x 10(-4) mol/L.
引用
收藏
页码:2850 / 2854
页数:5
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