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  2. 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 ...

  3. 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 ...

  4. Hydrogen potassium ATPase - Wikipedia

    en.wikipedia.org/wiki/Hydrogen_potassium_ATPase

    The gastric hydrogen potassium ATPase or H + /K + ATPase is the proton pump of the stomach.It exchanges potassium from the intestinal lumen with cytoplasmic hydronium [2] and is the enzyme primarily responsible for the acidification of the stomach contents and the activation of the digestive enzyme pepsin [3] (see gastric acid).

  5. Intrinsic factor - Wikipedia

    en.wikipedia.org/wiki/Intrinsic_factor

    The optimum pH for its action is approximately 7. [10] Its concentration does not correlate with the amount of HCl or pepsin in the gastric juice, e.g., intrinsic factor may be present even when pepsin is largely absent. [11] The site of formation of the intrinsic factor varies in different species.

  6. Intracellular pH - Wikipedia

    en.wikipedia.org/wiki/Intracellular_pH

    Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...

  7. 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 .

  8. Aspergillopepsin I - Wikipedia

    en.wikipedia.org/wiki/Aspergillopepsin_I

    Aspergillopepsin I (EC 3.4.23.18, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, Aspergillus carboxyl proteinase, carboxyl proteinase, Aspergillus kawachii aspartic proteinase, Aspergillus saitoi acid proteinase, pepsin-type aspartic proteinase, Aspergillus niger acid proteinase, sumizyme AP, proctase P, denapsin ...

  9. Davenport diagram - Wikipedia

    en.wikipedia.org/wiki/Davenport_diagram

    Recall that the relationship represented in a Davenport diagram is a relationship between three variables: P CO 2, bicarbonate concentration and pH.Thus, Fig. 7 can be thought of as a topographical map—that is, a two-dimensional representation of a three-dimensional surface—where each isopleth indicates a different partial pressure or “altitude.”