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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    The effects of temperature on enzyme activity. Top: increasing temperature increases the rate of reaction (Q10 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.

  3. Heinz body - Wikipedia

    en.wikipedia.org/wiki/Heinz_body

    G6PD deficient red cells in combination with high levels of oxidants causes a cross-linking of sulfhydryl groups on globin chains which causes a denaturing and formation of Heinz body precipitates. [8] Heinz bodies can also be found in chronic liver disease. [9] Alpha-thalassemia. Normal adult hemoglobin is composed of two alpha and two beta ...

  4. Carbonic anhydrase - Wikipedia

    en.wikipedia.org/wiki/Carbonic_anhydrase

    Carbonic anhydrase is one of the fastest enzymes, and its rate is typically limited by the diffusion rate of its substrates. Typical catalytic rates of the different forms of this enzyme ranging between 10 4 and 10 6 reactions per second. [15] The uncatalyzed reverse reaction is relatively slow (kinetics in the 15-second range).

  5. 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.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    At the maximum reaction rate (V max) of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme. [1]: 8.4 V max is only one of several important kinetic parameters. The amount of substrate needed to achieve a given rate of reaction is also important.

  7. Superoxide dismutase - Wikipedia

    en.wikipedia.org/wiki/Superoxide_dismutase

    Superoxide is known to denature enzymes, oxidize lipids, and fragment DNA. [21] SODs catalyze the production of O 2 and H 2 O 2 from superoxide (O − 2), which results in less harmful reactants. When acclimating to increased levels of oxidative stress, SOD concentrations typically increase with the degree of stress conditions.

  8. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Beyond this limit the enzyme is saturated with substrate and the reaction rate ceases to increase. The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. Like other catalysts, enzymes do not alter the position of equilibrium between substrates and products. [1]

  9. Degmacyte - Wikipedia

    en.wikipedia.org/wiki/Degmacyte

    A degmacyte or bite cell is an abnormally shaped mature red blood cell with one or more semicircular portions removed from the cell margin, known as "bites". [1] [2] These "bites" result from the mechanical removal of denatured hemoglobin during splenic filtration as red cells attempt to migrate through endothelial slits from splenic cords into the splenic sinuses. [3]