Kinetic equations and ligand binding equations may be very similar. The four most widely employed kinetic formats are the Michaelis–Menten, Lineweaver–Burk, Eadie– Hofstee, and Hill. The effective binding range for a ligand with constant affinity is nearly 100-fold. At [L] ≤ 0.1Kd, binding becomes ineffective. At [L] ≥ 10Kd, binding approaches saturation. This effective binding range is easily remembered as the 2-log rule. The effect of positive cooperativity is to make the binding range narrower, so that saturation is approached below [L] = 10Kd, by changing the affinity for the ligand. The effect of negative cooperativity is to extend the binding range so that saturation is never approached under physiological concentrations of the ligand.
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© 2008 Springer Science+Business Media, LLC
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(2008). Enzyme Kinetics. In: Allosteric Regulatory Enzymes. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-72891-9_3
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DOI: https://doi.org/10.1007/978-0-387-72891-9_3
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