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- In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver–Burk plots to find additional kinetic constants. For example, when a set of v by [S] curves from an enzyme with a ping–pong mechanism (varying substrate A, fixed substrate B) are plotted in a Lineweaver–Burk plot, a set of parallel lines will be produced. The following Michaelis–Menten equation relates the initial reaction rate v0 to the substrate concentrations [A] and [B]: The y-intercept of this equation is equal to the following: The y-intercept is determined at several different fixed concentrations of substrate B (and varying substrate A). The y-intercept values are then plotted versus 1/[B] to determine the Michaelis constant for substrate B, , as shown in the Figure to the right. The slope is equal to divided by and the intercept is equal to 1 over . (en)
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- 2937 (xsd:nonNegativeInteger)
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- In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver–Burk plots to find additional kinetic constants. For example, when a set of v by [S] curves from an enzyme with a ping–pong mechanism (varying substrate A, fixed substrate B) are plotted in a Lineweaver–Burk plot, a set of parallel lines will be produced. The following Michaelis–Menten equation relates the initial reaction rate v0 to the substrate concentrations [A] and [B]: The y-intercept of this equation is equal to the following: (en)
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- Secondary plot (kinetics) (en)
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