The thermokinetic reduced extent equations of reversible inhibitions for Michaiels-Menten enzymatic reaction were deduced, and then the criteria for distingushing inhibition type was given and the methods for calculat...The thermokinetic reduced extent equations of reversible inhibitions for Michaiels-Menten enzymatic reaction were deduced, and then the criteria for distingushing inhibition type was given and the methods for calculating kinetic parameters, KM,Ki and Urn were suggested. This theory was applied to inverstigate the inhibited thermokinetics of laccase-catalyzed oxidation of o-dihydroxybenzene by m-dihydroxybenzene. The experimental results show the inhibition belongs to reversible competitive type, KM=6.224×10-3 mol L-1, Ki=2. 363 × 10-2 mol. L-1.展开更多
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 co...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+ .展开更多
文摘The thermokinetic reduced extent equations of reversible inhibitions for Michaiels-Menten enzymatic reaction were deduced, and then the criteria for distingushing inhibition type was given and the methods for calculating kinetic parameters, KM,Ki and Urn were suggested. This theory was applied to inverstigate the inhibited thermokinetics of laccase-catalyzed oxidation of o-dihydroxybenzene by m-dihydroxybenzene. The experimental results show the inhibition belongs to reversible competitive type, KM=6.224×10-3 mol L-1, Ki=2. 363 × 10-2 mol. L-1.
基金ProjectsupportedbytheNaturalScienceFoundationofShandongProvince (No .Y2 0 0 0B0 3 )
文摘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+ .
