Scatchard diagram

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In addition to the Hill diagram, the Scatchard plot is a way of checking enzyme activity for cooperativity , i.e. answering the question of whether the enzyme has a higher or lower affinity for other ligands after binding a first ligand. (The Eadie-Hofstee diagram shows the same thing with the axes reversed.)

If you look at the equation for enzyme saturation

reshaped after

the form for the Scatchard plot is obtained. Y is the saturation and [L] the ligand concentration , K stands for the dissociation constant and Y max for the maximum possible enzyme saturation. Concentrations are often measured in M = mol / l , where nM or µM are typical orders of magnitude.

Some diagrams. The Scatchard chart is in the center right

Shape of the graph

An approximately linear plot is obtained with Y / [L] on the y-axis and Y on the x-axis, where -K −1 is the slope.

Information that can be read from the graph

  • In the case of a non- allosteric enzyme (the strength of the bond does not depend on the number of substrate or ligand molecules already bound) the diagram shows a linear decrease.
  • In the case of an allosteric, cooperatively working enzyme, a parabola that opens downwards is obtained.
  • In the case of negative cooperativity or non-identical, isolated binding sites, a concave course (curved to the right, or second derivative - so existent - negative) with a linear terminal branch arises .

The slopes here correspond to the affinities (-K d −1 or -K a ).

  • The total number of binding sites (active centers) can be read from the intersection with the x-axis.

See also

literature