1.Compared with control,HQ,PPD and NBPT made Km increase,and Vmax decrease,which indicates the mixed inhibition of tested urease inhibitors to soil urease.与对照相比,HQ、PPD和NBPT均使Km增加,Vmax降低,表明其作用机理均属于混合型抑制。 英文短句/例句 1.The application of membrane separation dehydration...
Apparent Km and Vmax values were calculated as 2.8 uM and 3.0 umol resorufin/min/mg protein based on Lineweaver-Burk plot of microsomal EROD activity, respectively. Diallyl disulfide (DADS) and diallyl trisulfide (DATS) affected Km and V max values of EROD activity and acted as mixed-type ...
When using it, Vmax, Km, Ki, and Alpha are shared, while Ic is a fixed constant. If Alpha=1, the mixed model is same as a noncompetitive inhibition model. If Alpha is very large, the mixed model is similar to a competitive inhibition model. If Alpha is very small, the mixed ...
2) mixed inhibition 混合型抑制 1. Compared with control,HQ,PPD and NBPT made Km increase,and Vmax decrease,which indicates the mixed inhibition of tested urease inhibitors to soil urease. 与对照相比,HQ、PPD和NBPT均使Km增加,Vmax降低,表明其作用机理均属于混合型抑制。 更多例句>> 3) pre-des...
Table 1. Kinetic parameters of native and mutant BPGH16 on various β glucans EnzymeSubstrateKm (mg ml−1)kcat (s−1)kcat/Km (s−1 mg−1 ml) BPGH16 Laminarin 0.24 ± 0.03 43 ± 0.6 179 Lichenan 0.13 ± 0.02 36 ± 0.5 275 Barley β-glucan 0.22 ± 0.04 62 ± 1.2 281 ...
362 INHIBITION OF MIXED FUNCTION OXIDASES (MFO) BY GROWTH HORMONE (GH) AND BY THE IMMUNOSTIMULANT CORYNE-BACTERIUM PARVUM (Cp): EVIDENCE FOR A COMMON MECHANISM Both GH and a variety of immunostimulants have been shown to inhibit MFO activity. We wished to determine whether the action of Cp ...
When using it, Vmax, Km, Ki, and Alpha are shared, while Ic is a fixed constant. If Alpha=1, the mixed model is same as a noncompetitive inhibition model. If Alpha is very large, the mixed model is similar to a competitive inhibition model. If Alpha is very small, the mixed model...
The kinetic behavior of enzyme hyase revealed to be more complex than classical competitive and uncompetitive inhibition where inhibitor affects both Km and Vmax. The inhibitor (I) favored the binding to the enzyme-substrate (ES) complex where Km value appeared to decrease (Kmapp < Km). The ...