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Enzyme activity. Enzyme activity is a measure of the quantity of active enzyme present and is thus dependent on various physical conditions, which should be specified. It is calculated using the following formula: where. = Enzyme activity. = Moles of substrate converted per unit time. = Rate of the reaction. = Reaction volume.
Enzyme unit. The enzyme unit, or international unit for enzyme (symbol U, sometimes also IU) is a unit of enzyme 's catalytic activity. [1] 1 U (μmol/min) is defined as the amount of the enzyme that catalyzes the conversion of one micro mole of substrate per minute under the specified conditions of the assay method. [2]
Molar concentration (also called molarity, amount concentration or substance concentration) is a measure of the concentration of a chemical species, in particular, of a solute in a solution, in terms of amount of substance per unit volume of solution. In chemistry, the most commonly used unit for molarity is the number of moles per liter ...
Dissociation constant. In chemistry, biochemistry, and pharmacology, a dissociation constant (KD) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its ...
Half maximal inhibitory concentration (IC50) is a measure of the potency of a substance in inhibiting a specific biological or biochemical function. IC 50 is a quantitative measure that indicates how much of a particular inhibitory substance (e.g. drug) is needed to inhibit, in vitro, a given biological process or biological component by 50% ...
To calculate molar ellipticity, the sample concentration (g/L), cell pathlength (cm), and the molecular weight (g/mol) must be known. If the sample is a protein, the mean residue weight (average molecular weight of the amino acid residues it contains) is often used in place of the molecular weight, essentially treating the protein as a solution ...
In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product. It takes the form of a differential equation describing the reaction rate (rate of formation of product P, with concentration ) to , the ...
The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.