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  2. Denaturation (biochemistry) - Wikipedia

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

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    The enzyme involved in this reaction is called invertase, and it is the enzyme the kinetics of which have been supported by Michaelis and Menten to be revolutionary for the kinetics of other enzymes. While expressing the rate of the reaction studied, they derived an equation that described the rate in a way which suggested that it is mostly ...

  4. Xylose isomerase - Wikipedia

    en.wikipedia.org/wiki/Xylose_isomerase

    [8]: 27 Many enzyme become denatured at these temperatures, and one focus of research has been engineering more thermostable versions of xylose isomerase and the other enzymes in the process. [8]: 27 [18] The enzymes are generally immobilized to increase throughput, and finding better ways to do this has been another research focus.

  5. Glycerol-3-phosphate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Glycerol-3-phosphate_de...

    Additionally, GPDH is one of the enzymes involved in maintaining the redox potential across the inner mitochondrial membrane. [3] Fig. 1. Schematic overview of fermentative and oxidative glucose metabolism of Saccharomyces cerevisiae. (A) upper part of glycolysis, which includes two sugar phosphorylation reactions. (B) fructose-1,6-bisphosphate ...

  6. Alcohol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Alcohol_dehydrogenase

    The ability to produce ethanol from sugar (which is the basis of how alcoholic beverages are made) is believed to have initially evolved in yeast. Though this feature is not adaptive from an energy point of view, by making alcohol in such high concentrations so that they would be toxic to other organisms, yeast cells could effectively eliminate ...

  7. Salting out - Wikipedia

    en.wikipedia.org/wiki/Salting_out

    Salt compounds dissociate in aqueous solutions. This property is exploited in the process of salting out. When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. [3]

  8. Deoxyribonuclease - Wikipedia

    en.wikipedia.org/wiki/Deoxyribonuclease

    A standard enzyme preparation should be run in parallel with an unknown because standardization of DNA preparations and their degree of polymerization in solution is not possible. Single Radial Enzyme Diffusion (SRED) This simple method for DNase I activity measurement was introduced by Nadano et al. and is based on the digestion of DNA in the ...

  9. Triosephosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Triosephosphate_isomerase

    Triose phosphate isomerase is a highly efficient enzyme, performing the reaction billions of times faster than it would occur naturally in solution. The reaction is so efficient that it is said to be catalytically perfect: It is limited only by the rate the substrate can diffuse into and out of the enzyme's active site. [2] [3]