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  2. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    Leucine ball and stick model spinning. Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side ...

  3. Leucines - Wikipedia

    en.wikipedia.org/wiki/Leucines

    The leucines are primarily the four isomeric amino acids: leucine, isoleucine, tert-leucine (terleucine, pseudoleucine) and norleucine. [1] Being compared with the four butanols, they could be classified as butyl-substituted glycines; they represent all four possible variations.

  4. Color of chemicals - Wikipedia

    en.wikipedia.org/wiki/Color_of_chemicals

    The color of chemicals is a physical property of chemicals that in most cases comes from the excitation of electrons due to an absorption of energy performed by the chemical. The study of chemical structure by means of energy absorption and release is generally referred to as spectroscopy .

  5. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.

  6. Protein digestibility corrected amino acid score - Wikipedia

    en.wikipedia.org/wiki/Protein_Digestibility...

    [3] [8] [9] This is because in 1990 at a FAO/WHO meeting, it was decided that proteins having values higher than 1.0 would be rounded or "leveled down" to 1.0 as scores above 1.0 are considered to indicate the protein contains essential amino acids in excess of the human requirements. [10]

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase. [18] Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its pathway also can inhibit the synthesis of leucine.

  8. Colorimetric analysis - Wikipedia

    en.wikipedia.org/wiki/Colorimetric_analysis

    The equipment required is a colorimeter, some cuvettes and a suitable color reagent. The process may be automated, e.g. by the use of an AutoAnalyzer or by flow injection analysis. Recently, colorimetric analyses developed for colorimeters have been adapted for use with plate readers to speed up analysis and reduce the waste stream. [1]

  9. Leucine (data page) - Wikipedia

    en.wikipedia.org/wiki/Leucine_(data_page)

    The complete data for Leucine ... Molar mass: 131.18 g·mol −1 Systematic name: (S ... Text is available under the Creative Commons Attribution-ShareAlike 4.0 ...