Enter your Maximum Velocity (Vmax), Michaelis Constant (Km), and substrate concentration range into the Hanes-Woolf Plot Calculator to generate your linearized enzyme kinetics curve — giving you the slope (1/Vmax), Y-intercept (Km/Vmax), and back-calculated Vmax and Km values straight from the plot.
Slope (1/Vmax)
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Y-Intercept (Km/Vmax)
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Calculated Vmax
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Calculated Km
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The y-intercept represents Km/Vmax, which is the ratio of the Michaelis constant to the maximum velocity. This value indicates the substrate concentration needed to achieve half-maximum velocity divided by the maximum velocity.
Hanes-Woolf linearization reduces error from low substrate concentration measurements compared to Lineweaver-Burk plots. It provides more accurate determination of kinetic parameters, especially when substrate concentrations are limited.
Vmax is calculated as the reciprocal of the slope (1/slope). Since the slope equals 1/Vmax in the Hanes-Woolf equation [S]/v = ([S]/Vmax) + (Km/Vmax), taking the inverse gives you the maximum velocity.
The slope of a Hanes-Woolf plot equals 1/Vmax. A steeper slope indicates a lower maximum velocity, while a gentler slope indicates a higher maximum velocity of the enzymatic reaction.
Km is calculated by multiplying the y-intercept by Vmax. Since the y-intercept equals Km/Vmax, multiplying by Vmax gives you the Michaelis constant: Km = y-intercept × Vmax.
The x-axis represents substrate concentration [S], and the y-axis represents the ratio [S]/v, where v is the reaction velocity. This creates a linear relationship that makes it easier to determine kinetic parameters.
Use Hanes-Woolf linearization when you need accurate enzyme kinetic parameters from experimental data, especially when dealing with low substrate concentrations. It's particularly useful when Lineweaver-Burk plots show too much scatter in the data.