Scatchard diagram
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.
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
- Enzyme kinetics for other such diagrams
literature
- Jeremy M. Berg, John L. Tymoczko, Lubert Stryer : Biochemistry. 6 edition, Spektrum Akademischer Verlag, Heidelberg 2007. ISBN 978-3-8274-1800-5 .
- Donald Voet, Judith G. Voet: Biochemistry. 3rd edition, John Wiley & Sons, New York 2004. ISBN 0-471-19350-X .