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LMDH-RO

Roche

L-Malate Dehydrogenase (L-MDH)

from pig heart (mitochondrial)

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352202

Source biologique

Porcine heart (mitochondrial)

Niveau de qualité

Forme

solution
suspension

Activité spécifique

~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.)

Conditionnement

pkg of 1 mL (10127248001 solution)
pkg of 1 mL (10127256001 suspension)
pkg of 5 mL (10127914001suspension)

Fabricant/nom de marque

Roche

Technique(s)

activity assay: suitable

Couleur

white

pH optimal

7.4-7.5(reduction of oxaloacetate)
9.2-9.5(oxidation of malate)

Solubilité

water: miscible

Adéquation

suitable for Western blot

Numéro d'accès NCBI

Numéro d'accès UniProt

Application(s)

life science and biopharma

Activité étrangère

Fumarase <0.01%
GIDH 0.001%
GOT 0.001%
GPT 0.00185%
LDH <0.01%
NADH oxidase <0.001%

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

Porcine ... MDH2(397039)

Description générale

L-malate:NAD+ oxidoreductase
The L-malate dehydrogenase enzyme is a nuclear gene product that is synthesized with a 24-residue amino-terminal signal peptide. This peptide is proteolytically cleaved during the translocation of the enzyme to the mitochondrial matrix.

Application

The enzyme L-malate dehydrogenase from pig heart has been used to measure PEPCK (phosphoenolpyruvate carboxykinase) activity. The oxaloacetate, produced by PEPCK, is reduced to malate via the oxidation of NADH, which in turn is measured at 340 nm using a spectrophotometer. The enzyme has also been used to measure oxaloacetate by measuring the reduction in NADH spectroscopically at 340 nm.

Actions biochimiques/physiologiques

The enzyme L-malate dehydrogenase from pig heart catalyzes the oxidation of L-malate to oxaloacetate. The enzyme is an NAD-dependent mitochondrial dehydrogenase that functions in the tricarboxylic acid cycle. It is a component of the malate-aspartate shuttle that transports reducing equivalents across the inner mitochondrial membrane in the form of malate.

Qualité

Contaminants: <0.002% GOT, <0.01% fumarase and LDH, each luM each, <0.02% HK, <0.002% PGI

Forme physique

Solution in 50% glycerol (v/v), pH approximately 7
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Notes préparatoires

Activator: – phosphate
– arsenate
– Mg2+
– Zn2+

Autres remarques

For life science research only. Not for use in diagnostic procedures.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

No data available

Point d'éclair (°C)

No data available


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Extraction and Measurement the Activities of Cytosolic Phosphoenolpyruvate Carboxykinase (PEPCK) and Plastidic NADP-dependent Malic Enzyme (ME) on Tomato (Solanum lycopersicum).
Osorio, S et al.
Bio-protocol, 4 (2014)
S L Roderick et al.
The Journal of biological chemistry, 261(20), 9461-9464 (1986-07-15)
In a previous study, we reported the apparent similarity between a low resolution electron density map of mitochondrial malate dehydrogenase and a model of cytoplasmic malate dehydrogenase (Roderick, S. L., and Banaszak, L. J. (1983) J. Biol. Chem. 258, 11636-11642).
Agata M Pudlik et al.
Journal of bacteriology, 193(3), 706-714 (2010-12-01)
Carbohydrate/citrate cometabolism in Lactococcus lactis results in the formation of the flavor compound acetoin. Resting cells of strain IL1403(pFL3) rapidly consumed citrate while producing acetoin when substoichiometric concentrations of glucose or l-lactate were present. A proton motive force was generated

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