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  2. Lactate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Lactate_dehydrogenase

    Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells. LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NAD + to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH exists in four distinct enzyme classes.

  3. Cardiac marker - Wikipedia

    en.wikipedia.org/wiki/Cardiac_marker

    Lactate dehydrogenase (LDH) LDH is not as specific as troponin. 72 hours Lactate dehydrogenase catalyses the conversion of pyruvate to lactate. LDH-1 isozyme is normally found in the heart muscle and LDH-2 is found predominantly in blood serum. A high LDH-1 level to LDH-2 suggest MI. LDH levels are also high in tissue breakdown or hemolysis.

  4. Gilbert's syndrome - Wikipedia

    en.wikipedia.org/wiki/Gilbert's_syndrome

    Cholestasis can be excluded by normal levels of bile acids in plasma, the absence of lactate dehydrogenase, low levels of conjugated bilirubin, and ultrasound scan of the bile ducts. [citation needed] Vitamin B12 deficiency - elevated bilirubin levels (and MCV counts above 90–92) can be associated with a vitamin B12 deficiency. [citation needed]

  5. Glutaminolysis - Wikipedia

    en.wikipedia.org/wiki/Glutaminolysis

    three ATP at a time for the NADH + H + produced within the α-ketoglutarate dehydrogenase reaction, the malate dehydrogenase reaction and the malate decarboxylase reaction. Due to low glutamate dehydrogenase and glutamate pyruvate transaminase activities, in tumor cells the conversion of glutamate to alpha-ketoglutarate mainly takes place via ...

  6. Anaerobic glycolysis - Wikipedia

    en.wikipedia.org/wiki/Anaerobic_glycolysis

    When sufficient oxygen is not present in the muscle cells for further oxidation of pyruvate and NADH produced in glycolysis, NAD+ is regenerated from NADH by reduction of pyruvate to lactate. [4] Lactate is converted to pyruvate by the enzyme lactate dehydrogenase. [3] The standard free energy change of the reaction is -25.1 kJ/mol. [6]

  7. Transudate - Wikipedia

    en.wikipedia.org/wiki/Transudate

    Transudates are caused by disturbances of hydrostatic or colloid osmotic pressure, not by inflammation. They have a low protein content in comparison to exudates and thus appear clearer. [6] Levels of lactate dehydrogenase (LDH) [7] or a Rivalta test can be used to distinguish transudate from exudate. [citation needed]

  8. Liver function tests - Wikipedia

    en.wikipedia.org/wiki/Liver_function_tests

    Lactate dehydrogenase (LDH) is found in many body tissues, including the liver. Elevated levels of LDH may indicate liver damage. [18] LDH isotype-1 (or cardiac) is used for estimating damage to cardiac tissue, although troponin and creatine kinase tests are preferred. [19]

  9. Hemolytic anemia - Wikipedia

    en.wikipedia.org/wiki/Hemolytic_anemia

    Laboratory studies commonly used to investigate hemolytic anemia include blood tests for breakdown products of red blood cells, bilirubin and lactate dehydrogenase, a test for the free hemoglobin binding protein haptoglobin, and the direct Coombs test (also called direct antiglobulin test or DAT) to evaluate complement factors and/or antibodies ...