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  2. Esophageal pH monitoring - Wikipedia

    en.wikipedia.org/wiki/Esophageal_pH_Monitoring

    Esophageal pH monitoring is performed for 24 or 48 hours and at the end of recording, a patient's tracing is analyzed and the results are expressed using six standard components. Of these 6 parameters, a pH score called Composite pH Score or DeMeester Score has been calculated, which is a global measure of esophageal acid exposure. A Demeester ...

  3. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...

  4. Acid phosphatase - Wikipedia

    en.wikipedia.org/wiki/Acid_phosphatase

    Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase .

  5. Acidophile - Wikipedia

    en.wikipedia.org/wiki/Acidophile

    Studies of proteins adapted to low pH have revealed a few general mechanisms by which proteins can achieve acid stability. In most acid stable proteins (such as pepsin and the soxF protein from Sulfolobus acidocaldarius), there is an overabundance of acidic residues which minimizes low pH destabilization induced by a buildup of positive charge ...

  6. Fecal pH test - Wikipedia

    en.wikipedia.org/wiki/Fecal_pH_test

    The pH of human faeces is variable but the average is pH 6.6 for normal faeces. [1] [2] A lower faecal pH (very acidic stool) can indicate a digestive problem such poor absorption of carbohydrates or fats, [3] lactose intolerance, [4] an infection such as E. coli or rotavirus, or overgrowth of acid-producing bacteria (such as lactic acid bacteria).

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  8. Aspartic protease - Wikipedia

    en.wikipedia.org/wiki/Aspartic_protease

    The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residue in the propeptide. This hydrogen bond stabilises the propeptide conformation and is probably responsible for triggering the conversion of pepsinogen to pepsin under acidic conditions.

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