Lineweaver-Burke equation

Equation 11-17 is refeiTed to as a Lineweaver-Burk equation involving separate dependent and independent variables 1/v and 1/Cg, respeetively. Equation 11-17 ean be further rearranged to give... 

The evaluation of the KM and vmax values for enzymatic reactions is usually carried out using a linear plot of Eq. 14. The Lineweaver-Burke equation is widely used to this aim ... 

FIGURE 17.5 Hie calibration curve of the electrocatalytic current on the concentration of glucose. Inset is the plot of Lineweaver-Burk equation. (From [253], with permission.)... 

Lineweaver-Burk equation, 14 627 Line widths, broadening, 23 131 Linewidth studies, 14 621-622 Linezolid, 3 26, 30, 36 17 733, 735 year of disclosure or market introduction, 3 6t... 

The Lineweaver-Burk equation is a reciprocal form of the Michaelis-Menten equation. The same data graphed in this way yield a straight line as shown in Figure 1-8-6. The actual data are represented by the portion of the graph to the right of the y-axis, but the line is extrapolated into the Idt quadrant to determine its intercept with the x-axis. The intercept of the line with the x-axis gives the value of The intercept of the line with the y-axis gives the value of... 

D. Although it may seem from Point B in Figure 3-3 that the can be determined from this representation of the velocity data, in practice, it is more accurate to use the Lineweaver-Burk equation, a modified form of the Michaelis-Menten equation, for estimation of and (Figure 3-4). 

Based on the Lineweaver-Burk equation, a plot of v versus 1/[S] gives a straight line on a Lineweaver-Burk or double reciprocal plot (Figure 3-4). 

This form of the Michaelis-Menten equation is called the Lineweaver-Burk equation. For enzymes obeying the Michaelis-Menten relationship, a plot of 1/F0 versus 1/[S] (the double reciprocal of the V0 versus [S] plot we have been using to this point) yields a straight line (Fig. 1). This line has a slope of Km/Vmax, an intercept of 1/Fmax on the 1/F0 axis, and an intercept... 

Michaelis-Menten equation 204 dissociation constant (Kf) 205 Lineweaver-Burk equation 206... 

The Eadie-Hofstee Equation One transformation of the Michaelis-Menten equation is the Lineweaver-Burk, or double-reciprocal, equation. Multiplying both sides of the Lineweaver-Burk equation by Umax and rearranging gives the Eadie-Hofstee equation ... 

Equation E3.5 in this experiment can be used to determine / values, but hyperbolic plots are obtained. Can you convert Equation E3.5 into an equation that will yield a linear plot without going through all the changes necessary for the Scatchard equation Hint Study the conversion of the Michaelis-Menten equation to the Lineweaver-Burk equation. 

Kinetic analysis of tyrosinase and calculation of constants will be described using graphical analysis by the Michaelis-Menten equation, Lineweaver-Burk equation, or the direct linear curve. Procedures for preparing these graphs are described below. Alternatively, students may use available computer software to graph data and calculate kinetic constants. Recommended enzyme kinetic computer software packages include Enzyme... 

Beginning with the Lineweaver-Burk equation, derive the Eadie-Hofstee equation. Explain how it may be used to plot a straight line from expen mental rate data. How are V and K., calculated ... 

B 8. Show the mathematical steps required to derive the Lineweaver-Burk equation beginning with the Michaelis-Menten equation. 

The Lineweaver-Burk equation for simple linear non-competitive inhibition is ... 

Historically, enzyme kinetics were visualised using the Lineweaver-Burk equation, Equation 11.14, where l/rate is plotted against 1/[S] as seen in Fig. 11.11 A ... 

Before adequate computer hardware and software were widely available, fitting experimental kinetic data to a curve to determine Km and Vmax was a significant challenge. Lineweaver and Burk rearranged the Michaelis-Menten equation to form a new linear relationship, the Lineweaver-Burk equation (Equation 4.13).6... 

In addition to being easier to fit than the hyperbolic Michaelis-Menten equation, Lineweaver-Burk graphs clearly show differences between types of enzyme inhibitors. This will be discussed in Section 4.5. However, Lineweaver-Burk equations have their own distinct issues. Nonlinear data, possibly indicating cooperative multiunit enzymes or allosteric effects, often seem nearly linear when graphed according to a Lineweaver-Burk equation. Said another way, the Lineweaver-Burk equation forces nonlinear data into a linear relationship. Variations of the Lineweaver-Burk equation that are not double reciprocal relationships include the Eadie-Hofstee equation7 (V vs. V7[S]) (Equation 4.14) and the Hanes-Woolf equation8 ([S]/V vs. [S]) (Equation 4.15). Both are... 

Repeat Question 11, but graph the data as a linear, double reciprocal plot in the spirit of the Lineweaver-Burk equation (see Chapter 4). Plot l/ATm vs. 1 /(N/nt) and perform a linear regression to determine the best-fit line (Equation 4.a). The x-intercept corresponds to the KD of the DNA-netropsin complex. The KD value from this method should be more accurate than the estimation in Question 11. 

Using the Living Graphs for Equation 6-30 and the Lineweaver-Burk equation in Box 6-1, create Lineweaver-Burk (double-reciprocal) plots for all the cases in (a) and (b). When a = 2.0, does the x intercept move to the right or to the left If a = 2.0 and a = 3.0, does the x intercept move to the right or to the left ... 

We can use the Lineweaver-Burk equation for this, the reciprocals of the variables in Table 9.3 must be calculated and then plotted as shown in Fig. 9-12. (Ignore the asterisks in Fig. 9-12 they refer to Prob. 9.9.) (a) From the reciprocal of the ordinate intercept, Tmax = 160/nmol L-1 min-1, and (b) from the reciprocal of the abscissal intercept, Km = 60/nmol L l. 

For each of the four types of enzyme inhibition given in Table 9.1, derive the Lineweaver-Burk equations and draw archetypal graphs. 

To derive the Lineweaver-Burk equations, we proceed by simply taking the reciprocals of each side of the equations expressing v0 as a function of [S]0 in Table 9-1. The corresponding graphs of l/u0 versus l/[S]o have varying slopes, intercepts, or both as [I] is varied. Pure noncompetitive inhibition shows lines... 

For the Michaelis-Menten equation there are algebraic transformations, in addition to the Lineweaver-Burk equation, that yield straight line plots from enzyme kinetic data. One such plot is due to Eadie and Hofstee their equation takes the following form ... 

Multiply the Lineweaver-Burk equation by [S] ) on both sides of the equals sign. 

The reciprocal of this equation, known as the Lineweaver-Burk equation (4), is shown in Equation 3. 

---