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L7525

Sigma-Aldrich

L-Lactic Dehydrogenase from porcine heart

ammonium sulfate suspension, ≥200 units/mg protein

Synonyme(s) :

(S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD, Lactate

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Porcine heart

Niveau de qualité

Forme

ammonium sulfate suspension

Activité spécifique

≥200 units/mg protein

Numéro d'accès UniProt

Activité étrangère

glutamic-oxalacetic transaminase ≤0.1%
malic dehydrogenase, glutamic-pyruvic transaminase and pyruvate kinase ≤0.06%

Température de stockage

2-8°C

Informations sur le gène

Description générale

Research area: Cell Signaling

Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).

Application

L-Lactic Dehydrogenase from porcine heart has been used:
  • as a component of the reaction buffer to measure the GTPase activity of EngA bound to the bacterial 50S subunit to study its structure and function.
  • as a component of the enzyme solutions to test the sensitivity of multiphoton NAD(P)H fluorescence lifetime imaging (FLIM) in key enzymatic steps controlling the path of carbon from glucose uptake to electron transport chain (ETC) activity.

Actions biochimiques/physiologiques

Lactate dehydrogenase (LDH) enzyme is responsible for the conversion of pyruvate to lactate, during glycolysis under hypoxic conditions, while also converting NADH to NAD+. Moreover it acts as a crucial regulator of gluconeogenesis and DNA metabolism. Increased serum LDH levels are detected in conditions such as cancer, HIV infection, muscular dystrophy, megaloblastic anemia, extreme hypothermia, hepatitis, meningitis, hypoxia, etc.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Définition de l'unité

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Forme physique

Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Joe T Sharick et al.
Scientific reports, 8(1), 5456-5456 (2018-04-05)
While NAD(P)H fluorescence lifetime imaging (FLIM) can detect changes in flux through the TCA cycle and electron transport chain (ETC), it remains unclear whether NAD(P)H FLIM is sensitive to other potential fates of glucose. Glucose carbon can be diverted from
H P Schär et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 360(7), 795-807 (1979-07-01)
Lactate dehydrogenases from thermophilic bacilli (Bacillus stearothermophilus, Bacillus caldotenax) and from mesophilic bacilli (Bacillus X1, Bacillus subtilis) have been isolated by a two-step purification procedure. Only one type (LDH-P4) composed of four identical subunits (Mr 34 000 or 36 000)
M J Adams et al.
Proceedings of the National Academy of Sciences of the United States of America, 70(7), 1968-1972 (1973-07-01)
The binding of coenzyme and substrate are considered in relation to the known primary and tertiary structure of lactate dehydrogenase (EC 1.1.1.27). The adenine binds in a hydrophobic crevice, and the two coenzyme phosphates are oriented by interactions with the
Brian M Peters et al.
Infection and immunity, 82(2), 532-543 (2014-01-31)
Vulvovaginal candidiasis, caused primarily by Candida albicans, presents significant health issues for women of childbearing age. As a polymorphic fungus, the ability of C. albicans to switch between yeast and hyphal morphologies is considered its central virulence attribute. Armed with
José A Jara et al.
Journal of medicinal chemistry, 57(6), 2440-2454 (2014-02-27)
Tumor cells principally exhibit increased mitochondrial transmembrane potential (ΔΨ(m)) and altered metabolic pathways. The therapeutic targeting and delivery of anticancer drugs to the mitochondria might improve treatment efficacy. Gallic acid exhibits a variety of biological activities, and its ester derivatives

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocoles

Enzymatic Assay of L-Lactic Dehydrogenase (EC 1.1.1.27)

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