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What else can I help you with?
Hp of 97 vmax sx 700 triple?
i would say about 115-120 its the same as the sxr motor and they put out about that
How many horsepower Yamaha vmax 800?
150 horse give or take a couple depending on individual sleds
How do you estimate the value of Vmax for two different concentrations of the substrate?
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.
What was the formula to claculate ac power supply?
P=(Vmax * Imax)/2 * (theata v - theta i)
How can one calculate Vmax from a Lineweaver-Burk plot?
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.
When did Yamaha start making the VMAX?
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.
How effective is Vmax in delivering optimal performance and results?
Vmax is highly effective in delivering optimal performance and results.
How do you calculate Vmax and Km for enzyme activity data?
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.
How can one determine the maximum velocity (Vmax) from a Lineweaver-Burk plot?
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.
How does the uncompetitive inhibitor affect both the Km and Vmax values in enzyme kinetics?
An uncompetitive inhibitor affects both the Km and Vmax values in enzyme kinetics by decreasing the apparent Km value and reducing the Vmax value.
How does uncompetitive inhibition affect both the Km and Vmax values in enzyme kinetics?
Uncompetitive inhibition affects both the Km and Vmax values in enzyme kinetics by decreasing the apparent Km value without changing the Vmax value.
When substrate concentration is much greater than Km the rate of catalysis is almost equal to?
the maximum catalytic rate (Vmax). At this point, all enzyme active sites are saturated with substrate and increasing the substrate concentration will not further increase the rate of catalysis.
