lactate dehydrogenase

(redirected from Lactate dehydrogenases)
Also found in: Dictionary, Encyclopedia.
Related to Lactate dehydrogenases: lactate dehydrogenase test

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 ?
Testis-specific lactate dehydrogenase (LDH-C4; Ldh3) in murine oocytes and preimplantation embryos.
Multiple splice variants of lactate dehydrogenase C selectively expressed in human cancer.
Lactate dehydrogenase isoenzymes A (muscle), B (heart) and C (testis) of mammals and the genes coding for these enzymes.
Muronetz, "Phosphorylation of lactate dehydrogenase by protein kinase," Biochemistry, vol.65, no.
Chung et al., "Tyrosine phosphorylation of lactate dehydrogenase a is important for NADH/[NAD.sup.+] redox homeostasis in cancer cells," Molecular and Cellular Biology, vol.
Epidermal growth factor regulates glucose metabolism through lactate dehydrogenase A messenger ribonucleic acid expression in cultured porcine Sertoli cells.
Nature and development of lactate dehydrogenase. Science 136:962-969.
Lactate dehydrogenase: biochemistry and function of lactate dehydrogenase.
de Jong, "Duck lens [epsilon]-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene pro duct with two distinct functions," Proceedings of the National Academy of Sciences of the United States of America, vol.
Krettli, "Antimalarial activity of potential inhibitors of Plasmodium falciparum lactate dehydrogenase enzyme selected by docking studies," PLoS ONE, vol.
An unusual isozyme of lactate dehydrogenase in mature testes: localization, ontogeny and kinetic properties.
Localization of total poteins and lactate dehydrogenase in hamster epididymis.

Full browser ?