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  2. Agarose gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Agarose_gel_electrophoresis

    A number of factors can affect the migration of nucleic acids: the dimension of the gel pores (gel concentration), size of DNA being electrophoresed, the voltage used, the ionic strength of the buffer, and the concentration of intercalating dye such as ethidium bromide if used during electrophoresis. [11]

  3. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    9 Factors affecting enzyme activity. ... which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, ...

  6. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  7. Control coefficient (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Control_coefficient...

    In biochemistry, control coefficients [1] are used to describe how much influence a given reaction step has on the flux or concentration of the species at steady state.This can be accomplished experimentally by changing the expression level of a given enzyme and measuring the resulting changes in flux and metabolite levels.

  8. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]

  9. Ligation (molecular biology) - Wikipedia

    en.wikipedia.org/wiki/Ligation_(molecular_biology)

    The concentration of DNA can affect the rate of ligation, and whether the ligation is an inter-molecular or intra-molecular reaction. Ligation involves joining up the ends of a DNA with other ends, however, each DNA fragment has two ends, and if the ends are compatible, a DNA molecule can circularize by joining its own ends.