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Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...
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.
The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.
Alternative online IC50 calculator (www.ic50.org) based on Python, NumPy, SciPy and Matplotlib; ELISA IC50/EC50 Online Tool (link seems broken) IC50 to pIC50 calculator; Online tool for analysis of in vitro resistance to antimalarial drugs; IC50-to-Ki converter of an inhibitor and enzyme that obey classic Michaelis-Menten kinetics
Specific activity (symbol a) is the activity per unit mass of a radionuclide and is a physical property of that radionuclide. [ 1 ] [ 2 ] It is usually given in units of becquerel per kilogram (Bq/kg), but another commonly used unit of specific activity is the curie per gram (Ci/g).
The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.
Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions involving the transformation of one substrate into one product.
While the Lineweaver–Burk plot has historically been used for evaluation of the parameters, together with the alternative linear forms of the Michaelis–Menten equation such as the Hanes–Woolf plot or Eadie–Hofstee plot, all linearized forms of the Michaelis–Menten equation should be avoided to calculate the kinetic parameters ...