No abstract available.
Kinetics* ; Wrist*

The Michaelis-Menten equation is one of the best-known models describing the enzyme kinetics of in vitro drug elimination experiments, and takes a form of equation relating reaction rate (V) to the substrate concentration ([S]) via the maximum reaction rate (Vmax) and the Michaelis constant (Km). The current study was conducted to compare the accuracy and precision of the parameter estimates in the Michaelis-Menten equation from various estimation methods using simulated data. One thousand replicates of simulated [S] over serial time data were generated using the results of a previous study, incorporating additive or combined error models as a source of random variables in the Monte-Carlo simulation using R. From each replicate of simulated data, Vmax and Km were estimated by five different methods, including traditional linearization methods and nonlinear ones without linearization using NONMEM. The relative accuracy and precision of the estimated parameters were compared by the median values and their 90% confidence intervals. Overall, Vmax and Km estimation by nonlinear methods (NM) provided the most accurate and precise results from the tested 5 estimation methods. The superiority of parameter estimation by NM was even more evident in the simulated data incorporating the combined error model. The current simulation study suggests that NMs using a program such as NONMEM provide more reliable and accurate parameter estimates of the Michaelis-Menten equation than traditional linearization methods in in vitro drug elimination kinetic experiments.
In Vitro Techniques ; Kinetics ; Methods

Fructose 1,6 bisphosphate adolase A and C (FPA A4 and C44) have been found to bind specifically to heparin in physiological ionic strength. The researcher found that activity of FPA was inhibited by heparin. The inhibition of FPA A4 and C4 depend on the degree of sulfation. Inhibition activity FPA of heparin increase directly proportional to molecule lenghth. Kinetic studies showed that: inhibitory mode of heparin on FPA was the linear mixed type inhibition, in which velocity can be driven to zero at high heparin concentration
Kinetics ; Fructose-Bisphosphate Aldolase ; Heparin

No abstract available.
Bromodeoxyuridine* ; Hep G2 Cells* ; Kinetics* ; Tretinoin*

Three-dimensional thermoluminescence (TL) spectra from MgAl2O4 irradiated with UV light were measured over 300~600 K and 300~800 nm. The peak positions of TL glow curves were shifted to lower temperature with increasing the exposure time of UV light. The 476 K TL glow curve is due to the second kinetics and its activation energy and escape frequency factor are calculated to be 0.85 eV and 1.92x10(6) sec(-1), respectively. The TL spectra were split into 530 nm and 700 nm emission bands which were associated with V(2+) and Cr(2+), respectively. The linearity range of 700 nm emission band is smaller than that of 530 nm emission band, but the saturation time of 700 nm emission band is longer than that of 530 nm emission band.
Aluminum* ; Kinetics ; Magnesium* ; Ultraviolet Rays ; United Nations

BACKGROUND: To determine the influence of lifting speed and type on peak and cumulative back compressive force (BCF) and shoulder moment (SM) loads during symmetric lifting. Another aim of the study was to compare static and dynamic lifting models. METHODS: Ten male participants performed a floor-to-shoulder, floor-to-waist, and waist-to-shoulder lift at three different speeds [slow (0.34 m/s), medium (0.44 m/s), and fast (0.64 m/s)], and with two different loads [light (2.25 kg) and heavy (9 kg)]. Two-dimensional kinematics and kinetics were determined. A three-way repeated measures analysis of variance was used to calculate peak and cumulative loading of BCF and SM for light and heavy loads. RESULTS: Peak BCF was significantly different between slow and fast lifting speeds (p < 0.001), with a mean difference of 20% between fast and slow lifts. The cumulative loading of BCF and SM was significantly different between fast and slow lifting speeds (p < 0.001), with mean differences > or =80%. CONCLUSION: Based on peak values, BCF is highest for fast speeds, but the BCF cumulative loading is highest for slow speeds, with the largest difference between fast and slow lifts. This may imply that a slow lifting speed is at least as hazardous as a fast lifting speed. It is important to consider the duration of lift when determining risks for back and shoulder injuries due to lifting and that peak values alone are likely not sufficient.
Biomechanics ; Humans ; Kinetics ; Lifting* ; Male ; Shoulder

No abstract available.
DNA* ; Kinetics* ; Nervous System Neoplasms* ; Nervous System*

The kinetics of inhibition of Na-K-ATPase activity by o, 0-dimethyl o-(2,2-dichlorovinyl) phosphate(DDVP) was investigated with homogenerate of rabbit cerebral cortex. The results were summarized as the follows : 1. Inhibition of Na-K-ATPase activity by DDVP showed a dose-dependent manner with an estimated I5.0 of 3.5x10(-4) M. 2. Altered pH and activity curves for Na-K-ATPase activity demonstrated comparable inhibition by DDVP in buffered acidic, neutral and alkaline pH renges. 3. Kinetic studies of cationic-substrate activation of Na-K-ATPase showed noncompetitive with respect to substrate and K+ and a mixed type inhibition with respect to Na+. These results suggest that DDVP appeared to exert its effects on Na-K-ATPase activity by interfering with the formation of Na-dependent phosphoenzyme.
Cerebral Cortex* ; Dichlorvos* ; Hydrogen-Ion Concentration ; Kinetics

Phosphoprotein Phosphatases ; Kinetics ; Protein Phosphatase 2/metabolism*

Genistein and its monoglucoside derivatives play important roles in food and pharmaceuticals fields, whereas their applications are limited by the low water solubility. Glycosylation is regarded as one of the effective approaches to improve water solubility. In this paper, the glycosylation of sophoricoside (genistein monoglucoside) was investigated using a cyclodextrin glucosyltransferase from Penibacillus macerans (PmCGTase). Saturation mutagenesis of D182 from PmCGTase was carried out. Compared with the wild-type (WT), the variant D182C showed a 13.42% higher conversion ratio. Moreover, the main products sophoricoside monoglucoside, sophoricoside diglucoside, and sophoricoside triglucoside of the variant D182C increased by 39.35%, 56.05% and 64.81% compared with that of the WT, respectively. Enzymatic characterization showed that the enzyme activities (cyclization, hydrolysis, disproportionation) of the variant D182C were higher than that of the WT, and the optimal pH and temperature of the variant D182C were 6 and 40℃, respectively. Kinetics analysis showed the variant D182C has a lower K_m value and a higher k_cat/K_m value than that of the WT, indicating the variant D182C has enhanced affinity to substrate. Structure modeling and docking analysis demonstrated that the improved glycosylation efficiency of the variant D182C may be attributed to the increased interactions between residues and substrate.
Cyclodextrins ; Genistein ; Glucosyltransferases/metabolism* ; Glycosylation ; Kinetics