Lineweaver-Burk double-reciprocal plot

Because of the hyperbolic shape of versus [S] plots, Vmax only be determined from an extrapolation of the asymptotic approach of v to some limiting value as [S] increases indefinitely (Figure 14.7) and is derived from that value of [S] giving v= V(nax/2. However, several rearrangements of the Michaelis-Menten equation transform it into a straight-line equation. The best known of these is the Lineweaver-Burk double-reciprocal plot ... 

FIGURE 14.9 The Lineweaver-Burk double-reciprocal plot, depicting extrapolations that allow the determination of the and 31-intercepts and slope. 

A Scatchard plot of the data is shown in Figure 5.10C. For convenience, the fitted line is the regression of B/F on B (though, as noted earlier, this is statistically unsound) and provides an estimate for Bmax ( -intercept) of 0.654 fmol/mg dry wt. and an estimate for KL (-1/slope) of 132 pM. A Lineweaver-Burk (double-reciprocal) plot is provided for comparison in Figure 5.10D. Linear regression gives another estimate for Bmax (I v-intercept see Eq. (5.29)) of 0.610 fmol/mg dry wt. The estimate of KL from this plot (slope x Bmax) is 114 pM. 

More accurate means of determining Km and Vmax are offered by either the Lineweaver-Burke (double reciprocal) plot or the Eadie-Hofstee plot (Figure 2.7). 

Figure 11. The Lineweaver-Burk double reciprocal plots of the FT Ni.

Figure 13. The Lineweaver-Burk double reciprocal plots of the FT Cu. Figure 14. The Lineweaver-Burk double reciprocal plots of the promoted Cu.

Equation 3.66 is, in fact, the Lineweaver-Burk double-reciprocal plot (equation 3.28) in slight disguise [E]0 has been moved to the left-hand side, and from equation 3.14, KM = ( , + k2)/kl. 

Fig. 4. The relationship between substrate concentration [S] and initial reaction velocity (V0). (a) A direct plot, (b) a Lineweaver-Burk double-reciprocal plot.

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 ... 

Effects of three types of reversible inhibitors on the velocity-substrate plots and on the Lineweaver-Burk double-reciprocal plots. 

Vm a is the maximal velocity for the reaction, and Km is a rate constant. Experimental determinations of Km and Vlna, are made with Lineweaver-Burk double-reciprocal plots. 

Analysis of eq. (6.114) shows, that Lineweaver-Burk double reciprocal plot (1/r v.s I/E0) is linear... 

ACTIVE FIGURE 6.10 A Lineweaver-Burk double-reciprocal plot of enzyme kinetics. The reciprocal of reaction velocity, 1/ T, is plotted against the reciprocal of the substrate concentration, 1/[S]. The slope of the line is and the y intercept is 1/V. The x inter-... 

ACTIVE FIGURE 6.12 A Lineweaver-Burk double-reciprocal plot of enzyme kinetics for competitive inhibition. Sign in at www.thomsonedu.com/iogin to see an interactive version of this figure. 

FIGURE 4.2 Lineweaver-Burk (double-reciprocal) plot of a reaction that follows Michaelis-Menten kinetics. Kinetic parameters are as defined previously. 

Fig. 3.5 Graphical representation of inhibition mechanisms in Lineweaver-Burke double reciprocal plots. Cl competitive inhibition NCI non-competitive inhibition UCI uncompetitive inhibition MTI mixed-type inhibition...

Figure 30.3 Lineweaver-Burke double reciprocal plot.

Figure 30.5 Lineweaver-Burke double reciprocal plot in the presence of competitive and non-competitive inhibitors.

Michaelis-Menten constant (Km) corresponds to the enzyme affinity subjected to biocatalysts, temperature, pH, and ionic strength of the biosensors. The higher value of Km implies the lower affinity, describing a slower process of substrate-enzyme binding. The Km is estimated in many different models however, Lineweaver-Burk (double reciprocal) plot is commonly applied in research studies. Considering these performance quantifications,... 

Figure 2.9 The Lineweaver—Burk double-reciprocal plot to determine and V. ...

Figure 2.10 The Lineweaver—Burk double-reciprocal plots for ordered and ping-pong two-substrate...

Figure 2.12 Substratehelocity and Lineweaver—Burk double-reciprocal plots for an enzyme incubated...

The competitive inhibition (Equation 5) and non-competitive inhibition (Equation 6) equations model different inhibitory processes and are easily identified using Lineweaver-Burk double reciprocal plots (Figure 3). Competitive inhibition has been defined as a direct... 

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