Lineweaver-Burk plot
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In biochemistry, the Lineweaver-Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver-Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934. The plot provides a useful graphical method for analysis of the Michaelis-Menten equation:
![V = V_{max}\frac{[S]}{K_m + [S]}](../../../math/1/3/a/13a6e707391eebde6b0c460f578572a5.png)
Taking the reciprocal gives
![{1 \over V} = {(K_m + [S]) \over (V_{max}[S])} = {K_m \over V_{max}} {1 \over [S]} + {1 \over V_{max}}](../../../math/6/4/0/6402a47707839ea3fc1c2f9ab7ff5395.png)
where V is the reaction velocity, Km is the Michaelis-Menten constant, Vmax is the maximum reaction velocity, and [S] is the substrate concentration.
The Lineweaver-Burk plot is useful for rapidly identifying important terms in enzyme kinetics, such as Km and Vmax. For instance, the y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents -1/Km.
As the double reciprocal plot distorts the error structure of the data it is unreliable. Most modern workers will either use non-linear regression or an alternative linear form of the Michaelis-Menten equation such as the Eadie-Hofstee plot.
[edit] Reference
- Lineweaver, H, and Burk, D. (1934). "The Determination of Enzyme Dissociation Constants". Journal of the American Chemical Society 56: 658—666.
