释义 |
lactate dehydrogenase
lactate dehydrogenasen. Abbr. LDH Any of a class of enzymes that catalyze the reversible interconversion of pyruvate and lactate, found predominantly in the liver, kidneys, skeletal muscle, heart muscle, and red blood cells.lac′tate dehy′drogenase n. an enzyme of carbohydrate metabolism that interchanges lactate and pyruvate: elevated blood levels indicate injury to kidney, heart, or muscles. Abbr.: LDH lactate dehydrogenase
lactate dehydrogenase[′lak‚tāt dē′hī·drə·jə‚nās] (biochemistry) A zinc-containing enzyme which catalyzes the oxidation of several α-hydroxy acids to corresponding α-keto acids. lactate dehydrogenase
lactate dehydrogenase (LD, LDH) [lak´tāt de-hi´dro-jĕ-nās] an enzyme that catalyzes the interconversion of lactate and pyruvate. It is widespread in tissues and is particularly abundant in kidney, skeletal muscle, liver, and myocardium. It has five isoenzymes denoted LD1 to LD5. The “flipped” pattern in which the serum LD1 level is greater than the LD2 level is indicative of an acute myocardial infarction. This pattern occurs within 12 to 24 hours after the attack.lac·tate de·hy·dro·gen·ase (LDH), name for a number of enzymes, including: l-lactate dehydrogenase (cytochrome), d-lactate dehydrogenase (cytochrome), l-lactate dehydrogenase, and d-lactate dehydrogenase. The first two enzymes transfer hydrogen to ferricytochrome c or to cytochrome b2, the last two transfer it to NAD+, in catalyzing the oxidation of lactate to pyruvate; the isozyme distribution of heart and muscle lactate dehydrogenase is of significant use in cases of myocardial infarction; a deficiency of a subunit will result in myoglobinuria after intense exercise. Synonym(s): lactic acid dehydrogenaselactate dehydrogenasen. Abbr. LDH Any of a class of enzymes that catalyze the reversible interconversion of pyruvate and lactate, found predominantly in the liver, kidneys, skeletal muscle, heart muscle, and red blood cells.lactate dehydrogenase Cardiology An oxidoreductase present in the cytoplasm of all cells that catalyze Lactate + NAD+ ↤ Pyruvate + NADH + H+, the equilibrium of which favors lactate + NAD+ at neutral pH; LD1 is classically ↑ in acute MI, peaking by post-infarct day 4, and associated with a flip in normal ratio of LD1 and LD2. See Flipped LD, LD6. Cf CK-MB, Troponin I, Troponin T. lac·tate de·hy·dro·gen·ase (LDH) (lak'tāt dē'hī-droj'ĕn-ās) Name for four enzymes. The first two transfer H to ferricytochrome c; the last two transfer it to NAD+, in catalyzing the oxidation of lactate to pyruvate; the isozyme distribution of heart and muscle lactate dehydrogenase is of diagnostic use in myocardial infarction. lactate dehydrogenase (LDH) One of the cell enzymes released into the blood when heart muscle cells are damaged during a heart attack (myocardial infarction). A measure of the concentration of these enzymes can indicate the severity of the attack.lac·tate de·hy·dro·gen·ase (LDH) (lak'tāt dē'hī-droj'ĕn-ās) Name for four enzymes; of diagnostic use in myocardial infarction. AcronymsSeeload highThesaurusSeelactate |