17 HMR and .17 Mach II are nice fast little rounds. The HMR is necked down from the .22 magnum the Mach II necked down from a .22 long rifle. They are nice target rounds and good for squirrels, rabbits, ground hogs and even coyote with a well placed shot if it's within 50 yards or longer distance for the .17 HMR. they would be good for raccoon if trapped or feral cats should the need arise. They could easily kill a 300 pound hog for butchering if shot behind the ear. They are little bullets, but very fast and still dangerous so be sure of your target and the region beyond.
If the enzyme concentration is increased by a factor of four, the Km value would remain the same because it is a property of the enzyme-substrate complex. The Vmax value would increase proportionally to the increase in enzyme concentration, also by a factor of four, due to more enzyme-substrate complexes being formed.
The Vmax would be the highest rate, when the enzyme is fully saturated. So as you increase substrate the Vmax will increase to a certain point (Vmax). Beyond that point, no matter how much substrate you add the Vmax will not increase.
To calculate Vmax from a Lineweaver-Burk plot, you can find the reciprocal of the y-intercept, which represents 1/Vmax. By taking the reciprocal of this value, you can determine the actual Vmax value.
Yamaha started making the VMAX in 2008. The VMAX, however, is no longer being manufactured in 2013 though and is out of production at the moment with no plans for future production.
Vmax is highly effective in delivering optimal performance and results.
To calculate Vmax and Km for enzyme activity data, you can use the Michaelis-Menten equation. Vmax is the maximum reaction rate of the enzyme, and Km is the substrate concentration at which the reaction rate is half of Vmax. By plotting a Lineweaver-Burk plot or a double reciprocal plot of the enzyme activity data, you can determine Vmax and Km by analyzing the slope and intercept of the line.
To determine the maximum velocity (Vmax) from a Lineweaver-Burk plot, you can find the y-intercept of the plot. Vmax is equal to the reciprocal of the y-intercept.
An uncompetitive inhibitor affects both the Km and Vmax values in enzyme kinetics by decreasing the apparent Km value and reducing the Vmax value.
Vmax is the maxim initial velocity (Vo) that an enzyme can achieve. Initial velocity is defined as the catalytic rate when substrate concentration is high, enough to saturate the enzyme, and the product concentration is low enough to neglect the rate of the reverse reaction. Therefore, the Vmax is the maximum catalytic rate that can be achieved by a particular enzyme. Km is determined as the substrate concentration at which 1/2 Vmax is achieved. This kinetic parameter therefore importantly defines the affinity of the substrate for the enzyme. These two parameters for a specific enzyme defines: Vmax - the rate at which a substrate will be converted to product once bound to the enzyme. Km - how effectively the enzyme would bind he substrate, hence affinity.
Uncompetitive inhibition affects both the Km and Vmax values in enzyme kinetics by decreasing the apparent Km value without changing the Vmax value.
i would say about 115-120 its the same as the sxr motor and they put out about that
Glucokinase