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  2. Histidinemia - Wikipedia

    en.wikipedia.org/wiki/Histidinemia

    A typical characteristic of histidinemia is an increase in the blood histidine levels from normal levels (70–120 μM) to an elevated level (290–1420 μM). [3] Further testing includes: observing histidine as well as imidazolepyruvic acid metabolites in the urine. However, neonatal urine testing has been discontinued in most places, with the ...

  3. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...

  4. Carnosinemia - Wikipedia

    en.wikipedia.org/wiki/Carnosinemia

    Carnosine is a dipeptide composed of beta-alanine and histidine, and is found in skeletal muscle and cells of the nervous system. [6] This disorder results in an excess of carnosine in the urine , cerebrospinal fluid , blood , and nervous tissue . [ 7 ]

  5. Reference ranges for blood tests - Wikipedia

    en.wikipedia.org/wiki/Reference_ranges_for_blood...

    Reference ranges (reference intervals) for blood tests are sets of values used by a health professional to interpret a set of medical test results from blood samples. Reference ranges for blood tests are studied within the field of clinical chemistry (also known as "clinical biochemistry", "chemical pathology" or "pure blood chemistry"), the ...

  6. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    Imidazole is the side chain of histidine and is typically used at a concentration of 150 - 500 mM for elution. Histidine or histamine can also be used. Decrease in pH; When the pH decreases, the histidine residue is protonated and can no longer coordinate the metal tag, allowing the protein to be eluted.

  7. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The triad of cytomegalovirus protease [b] uses histidine as both the acid and base triad members. Removing the acid histidine results in only a 10-fold activity loss (compared to >10,000-fold when aspartate is removed from chymotrypsin). This triad has been interpreted as a possible way of generating a less active enzyme to control cleavage ...

  8. Histidine decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Histidine_decarboxylase

    The enzyme histidine decarboxylase (EC 4.1.1.22, HDC) is transcribed on chromosome 15, region q21.1-21.2, and catalyzes the decarboxylation of histidine to form histamine. In mammals, histamine is an important biogenic amine with regulatory roles in neurotransmission , gastric acid secretion and immune response .

  9. Carnosine - Wikipedia

    en.wikipedia.org/wiki/Carnosine

    Carnosine (beta-alanyl-L-histidine) is a dipeptide molecule, made up of the amino acids beta-alanine and histidine. It is highly concentrated in muscle and brain tissues. [citation needed] Carnosine was discovered by Russian chemist Vladimir Gulevich. [1] Carnosine is naturally produced by the body in the liver [2] from beta-alanine and histidine.