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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, radiation, or heat. [3]

  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–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    An acid-base diagram for human plasma, showing the effects on the plasma pH when P CO 2 in mmHg or Standard Base Excess (SBE) occur in excess or are deficient in the plasma [23] Acid–base imbalance occurs when a significant insult causes the blood pH to shift out of the normal range (7.32 to 7.42 [ 16 ] ).

  5. Alkaline phosphatase - Wikipedia

    en.wikipedia.org/wiki/Alkaline_phosphatase

    The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase, also abbreviated PhoA) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found ...

  6. Lactic acidosis - Wikipedia

    en.wikipedia.org/wiki/Lactic_acidosis

    With high grain consumption, the concentration of dissociated organic acids can become quite high, resulting in rumen pH dropping below 6. Within this lower pH range, Lactobacillus spp. (producing lactate and hydrogen ions) are favored, and M. elsdenii and S. ruminantium are inhibited, tending to result in a considerable rise of lactate and ...

  7. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  8. Coagulative necrosis - Wikipedia

    en.wikipedia.org/wiki/Coagulative_necrosis

    The lack of lysosomal enzymes allows it to maintain a "coagulated" morphology for some time. Like most types of necrosis, if enough viable cells are present around the affected area, regeneration will usually occur. Coagulative necrosis occurs in most bodily organs, excluding the brain. [2]

  9. Metabolic acidosis - Wikipedia

    en.wikipedia.org/wiki/Metabolic_acidosis

    Metabolic acidosis is a serious electrolyte disorder characterized by an imbalance in the body's acid-base balance.Metabolic acidosis has three main root causes: increased acid production, loss of bicarbonate, and a reduced ability of the kidneys to excrete excess acids. [5]