Sentence examples for maximum enzyme velocity from inspiring English sources
Once the saturation is achieved (maximum enzyme velocity, νmax), any further addition of the substrate will not change the rate of reaction.
The Vmax and Km were calculated by non-linear fitting (Prism5 from GraphPad) using the equation: where V is the observed enzyme velocity (activity), Vmax is the maximum enzyme velocity, S is the substrate concentration, and Km is the Michaelis-Menten constant.
In order to determine whether the difference in renal ACE2 activity between males and females was due to differences in enzyme substrate affinity (Km) or to maximum enzyme velocity (Vmax), we calculated the Km and Vmax from ACE2 substrate dose response curves from 3.75 to 30 μM substrate concentration in male and female MF1 mice.
(2) (3) (4) (5) (6) where Vmax is the maximum enzyme velocity, Vapp the apparent maximal enzyme velocity, S the concentration of the substrate being varied, I the inhibitor concentration, K m the apparent Michelis Menten constant for S, S0.5 the half-saturation concentration for S, n the apparent Hill coefficient for S, Kis and Kii the dissociation constants of the [I] for E and ES, respectively.
In reactions conducted at substrate concentrations approaching or exceeding the Km, in which enzyme velocity approaches its maximum, V max, the non-linear relation of velocity to substrate concentration invalidates such simple corrections.
The classic MM equation describes the dependence of the enzyme velocity ν on substrate concentration [ S]. ν asymptotically approaches a maximum value (νmax) at high [ S] when enzymatic sites are saturated.
This strategy requires knowledge of maximal enzyme velocities (vmax).
On the other hand, the maximum reaction velocity, Vmax, values for the immobilized enzyme were remarkable; it was found to double that of the free enzyme; that is, it increased from 32.7 to 63.2 μmol·min−1.
U0126 is an irreversible inhibitor of MEK and functionally lowers the maximum velocity of this enzyme.
The concentrations of the substrates and co-enzymes in the incubation media were sufficiently high to ensure maximum velocity (Vmax) of the enzyme activities [ 26, 28].
Previously, Nunes and coworkers, [30] reported a higher Michaelis Menten constant (KM) and lower maximum reaction velocity (V max) for immobilized naringinase than that of free enzyme.
