منابع مشابه
Measurement of Michaelis Constants for ATP and Mg2+ in Bioluminescence Reaction of Luciferase by a Home-Made Luminometer
Effects of ATP and Mg2+ concentrations on bioluminescence reaction of luciferase (Photinus pyralis) were investigated by home-made luminometer. The Michaelis constants of the enzyme for ATP and Mg2+ obtained from the Lineweaver-Burk graph, were 61.9 mM ±3.3 mM and 251.6mM ± 39.0mM...
متن کاملMeasurement of Michaelis constants for cytochrome P450-mediated biotransformation reactions using a substrate depletion approach.
The Michaelis constant (KM) for cytochrome P450-mediated drug biotransformation reactions can be an important parameter in understanding the potential for a drug to exhibit saturable metabolism in vivo and nonlinear dose-exposure relationships. KM values were measured for several drug biotransformation reactions using recombinant heterologously expressed human enzymes. These determinations were...
متن کاملOn oxygen diffusion in a spherical cell with Michaelis-Menten oxygen uptake kinetics.
describes the steady-state oxygen diffusion in a spherical cell with MichaelisMenten oxygen uptake kinetics (Lin, 1976; McElwain, 1978). Throughout the paper, primes denote differentiation with respect to r. A l l quantities in (1) and (2) are dimensionless, where the normalized variables C and r represent the oxygen tension and the radial distance. The radius of the cell corresponds to r = 1, ...
متن کاملmeasurement of michaelis constants for atp and mg2+ in bioluminescence reaction of luciferase by a home-made luminometer
effects of atp and mg2+ concentrations on bioluminescence reaction of luciferase (photinus pyralis) were investigated by home-made luminometer. the michaelis constants of the enzyme for atp and mg2+ obtained from the lineweaver-burk graph, were 61.9 mm ±3.3 mm and 251.6mm ± 39.0mm respectively. optimum concentration of mg2+ for maximum luminescence was 0.004 m.
متن کاملA Comparison of Estimates of Michaelis-Menten Kinetic Constants from Various Linear Transformations
The parameters which characterize this equation, and which must ordinarily be estimated from the observed data, are ‘v,,,, the maximum initial velocity which is theoretically attained when the enzyme has been “saturated” by an infinite concentration of substrate, and K,, the Michaelis constant which is numerically equal to the concentration of substrate for half-maximal initial velocity. Since ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1993
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2930859