摘要
Intrinsic fluorescence emission maxima of hemoglobin(Hb) was investigated in relation to peroxidase property of Hb. The peroxidase activity of Hb was based on its ca\| talytic activity for oxidation of o \|phenylenediamine by hydrogen peroxide. Hb was treated in the condition (temperature, ethanol and salt) that tetramer\|dimer equilibrium of Hb is shifted to the dimer state and its fluorescence spectrum was measured . When Hb treated in temperature (60\|70 ℃), ethanol concentration (60%\|70%) and NaCl concentration (2.5\|3.0 mol/L), the fluorescence emission maxima of Hb shifted towards red wavelength and its activity decreased quickly. Experimental results revealed that the activity and stability of Hb as mimetic peroxidase was closely relative to the hydrophobic environment of active center of Hb, and when Hb (Fe Ⅱ ) converted into met Hb (Fe Ⅲ ), its activity was 1.6 times as much as that of Hb.
Intrinsic fluorescence emission maxima of hemoglobin(Hb) was investigated in relation to peroxidase property of Hb. The peroxidase activity of Hb was based on its ca\| talytic activity for oxidation of o \|phenylenediamine by hydrogen peroxide. Hb was treated in the condition (temperature, ethanol and salt) that tetramer\|dimer equilibrium of Hb is shifted to the dimer state and its fluorescence spectrum was measured . When Hb treated in temperature (60\|70 ℃), ethanol concentration (60%\|70%) and NaCl concentration (2.5\|3.0 mol/L), the fluorescence emission maxima of Hb shifted towards red wavelength and its activity decreased quickly. Experimental results revealed that the activity and stability of Hb as mimetic peroxidase was closely relative to the hydrophobic environment of active center of Hb, and when Hb (Fe Ⅱ ) converted into met Hb (Fe Ⅲ ), its activity was 1.6 times as much as that of Hb.
基金
theNationalNaturalScienceFoundationofChina (39770 2 0 0 )
