摘要
With or without activation or inhibition of metal ion,the power-time curves of amylase catalyzed reaction were determined by a 2277 thermal activity monitor (Sweden). The Michaelis constant ( K ),apparent Michaelis constant ( K _m),maximum velocity ( v _m) and apparent maximum velocity ( v _ am ) of amylase catalyzed reaction were obtained using thermokinetic theory and reduced extent method. On the basis of data obtained,the following relationships between K _m and concentration of metal ion ( c ) were established: for inhibitor of Ni 2+ K _m=2.9648×10 -3 -1.3912×10 -4 cR =0.9998for inhibitor of Co 2+ K _m=1.0227×10 -3 +8.2676×10 -6 cR =0.9955for activator of Ca 2+ K _m=1.0630×10 -7 c 2-1.8311×10 -6 c +9.3058×10 -6 R =0.9999for activator of Li + K _m=5.6300×10 -8 c 2-1.5329×10 -6 c +1.2662×10 -5 R =0.9999 The K _m- c relationships show a strenuous inhibitory effect for Ni 2+ and a strenuous active effect for Ca 2+ .
With or without activation or inhibition of metal ion,the power-time curves of amylase catalyzed reaction were determined by a 2277 thermal activity monitor (Sweden). The Michaelis constant ( K ),apparent Michaelis constant ( K _m),maximum velocity ( v _m) and apparent maximum velocity ( v _ am ) of amylase catalyzed reaction were obtained using thermokinetic theory and reduced extent method. On the basis of data obtained,the following relationships between K _m and concentration of metal ion ( c ) were established: for inhibitor of Ni 2+ K _m=2.9648×10 -3 -1.3912×10 -4 cR =0.9998for inhibitor of Co 2+ K _m=1.0227×10 -3 +8.2676×10 -6 cR =0.9955for activator of Ca 2+ K _m=1.0630×10 -7 c 2-1.8311×10 -6 c +9.3058×10 -6 R =0.9999for activator of Li + K _m=5.6300×10 -8 c 2-1.5329×10 -6 c +1.2662×10 -5 R =0.9999 The K _m- c relationships show a strenuous inhibitory effect for Ni 2+ and a strenuous active effect for Ca 2+ .
基金
ProjectsupportedbytheNaturalScienceFoundationofShandongProvince (No .Y2 0 0 0B0 3 )
