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Nafcillin uptake by human hepatocytes was saturable with a Km of 533 μM.
Kinetic analysis indicated that 8 binds with a Km value of 210 μM and a catalytic turnover rate, kcat of 52 s−1.
In kinetic analysis, 1 was found to be a good substrate with a Km of 23.7 μM and a Vmax of 159 pmol/h.
Heterologous isomerase activities in cell extracts, assayed at 30°C, were 0.3 1.1 μmol min−1 (mg protein)−1, with a Km for xylose of 20 mM.
Our kinetic data show that hypoxanthine is the substrate with highest affinity for the enzyme with a Km well below 1 μM.
The 6×His-rGalE with a Km of 0.5 mM for UDP-galactose exhibited optimum activity at 37 °C and pH 8 9.
hENT1 transports the substrate adenosine with a Km of 215 ± 34 µmol/L and a Vmax of 578 ± 23.4 nmol mg−1 mg−11.
Pre-treatment with 10− 4 M amiloride exposed a net outward (negative) ISC, and serosal NH4+ addition further increased this outward current with a Km of 53 ± 24 mM.
Initial velocities of DA uptake were kinetically resolved and displayed Michaelis Menten kinetics with a Km and Vmax of 289 ± 59 nM and 1.9 ± 0.2 fmol/(s μg protein), respectively.
It has been shown that a commercially available pectinase, Pectinex™, hydrolyzes chitin fairly efficiently with a Km of 2.2 mg ml−1 of chitin and Vmax equal to 6.5 nmol min−1 min−1
Bilateral addition of NH4+ caused a dose-dependent outward current (negative ISC), with a Km of 34 ± 8 mM and a maximal current response of 311 ± 47 µA cm− 2 (12 ± 2 µEq cm− 2 h− 1).
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