lactate dehydrogenase


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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.

lactate dehydrogenase

n. 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.
References in periodicals archive ?
Diagnostic value of ascetic fluid lactate dehydrogenase, protein and WBC levels.
The association of serum lactate dehydrogenase level with selected opportunistic infections & HIV progression.
Moreover, the detection of the presence of the MCT1 mitochondrial isoform in the plasma membrane and of intra-mitochondrial lactate dehydrogenase enzyme (intramitochondrial LDH) (12,13) led to a new interpretation of the monocarboxylate transporters where cytosolic lactate could be captured and re-oxidized in the mitochondria within the same cell (6).
This study revealed that lactate dehydrogenase was insignificantly higher in serum.
Normalized lactate dehydrogenase results for HAEC female treated with antioxidants also resulted in significant differences.
We further tested those malaria antibody positives with the pLDH CELISA kit to detect plasmodium specific lactate dehydrogenase enzyme.
Wang et al., "Lactate dehydrogenase B is critical for hyperactive mTOR-mediated tumorigenesis," Cancer Research, vol.
falciparum lactate dehydrogenase (PfLDH) is essential for the anaerobic lifestyle of Plasmodium and a potential drug target [86].
We have also observed morphological changes and release of lactate dehydrogenase into the medium upon treatment of DRG neurons with manganese chloride.
We read with interest the commentary of Gao (1) regarding our letter about the possible value of serum lactate dehydrogenase (LDH) as an early marker of posterior encephalopathy syndrome (2).

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