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Whereas the IC 50 value for a compound may vary between experiments depending on experimental conditions, (e.g. substrate and enzyme concentrations) the K i is an absolute value. K i is the inhibition constant for a drug; the concentration of competing ligand in a competition assay which would occupy 50% of the receptors if no ligand were present.
Toxic units (TU) are used in the field of toxicology to quantify the interactions of toxicants in binary mixtures of chemicals. [1] A toxic unit for a given compound is based on the concentration at which there is a 50% effect (ex. EC50) for a certain biological endpoint.
The term "potency" refers to the EC 50 value. The lower the EC 50, the less the concentration of a drug is required to produce 50% of maximum effect and the higher the potency. The EC 10 and EC 90 concentrations to induce 10% and 90% maximal responses are defined similarly.
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Ligand efficiency is a measurement of the binding energy per atom of a ligand to its binding partner, such as a receptor or enzyme. [1]Ligand efficiency is used in drug discovery research programs to assist in narrowing focus to lead compounds with optimal combinations of physicochemical properties and pharmacological properties.
The botulinum toxin as the most toxic substance known has an LD 50 value of 1 ng/kg, while the most non-toxic substance water has an LD 50 value of more than 90 g/kg; a difference of about 1 in 100 billion, or 11 orders of magnitude. As with all measured values that differ by many orders of magnitude, a logarithmic view is advisable.
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Virus quantification is counting or calculating the number of virus particles (virions) in a sample to determine the virus concentration. It is used in both research and development (R&D) in academic and commercial laboratories as well as in production situations where the quantity of virus at various steps is an important variable that must be monitored.