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LMDH-RO

Roche

L-Malate Dehydrogenase (L-MDH)

from pig heart (mitochondrial)

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About This Item

UNSPSC Code:
12352202
EC Number:
NACRES:
NA.54
Specific activity:
~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.)
Biological source:
Porcine heart (mitochondrial)
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biological source

Porcine heart (mitochondrial)

form

solution, suspension

specific activity

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

packaging

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

manufacturer/tradename

Roche

technique(s)

activity assay: suitable

color

white

optimum pH

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

solubility

water: miscible

suitability

suitable for Western blot

NCBI accession no.

UniProt accession no.

application(s)

life science and biopharma

foreign activity

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

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Porcine ... MDH2(397039)

General description

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.[1]

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.[2]

Biochem/physiol Actions

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.[1]

Physical form

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

Preparation Note

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

Analysis Note

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

Other Notes

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

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This Item
LLDH-ROM1567442610-M
Gene Information

Porcine ... MDH2(397039)

Gene Information

rabbit ... LOC100355262(100355262)

Gene Information

-

Gene Information

-

biological source

Porcine heart (mitochondrial)

biological source

rabbit muscle

biological source

-

biological source

Porcine heart

specific activity

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

specific activity

~550 units/mg protein (at 25 °C (1,100 U/mg at 37 °C) with pyruvate as the substrate.)

specific activity

≥600 units/mg protein (biuret)

specific activity

≥100 units/mg dry wt., ≥1000 units/mg protein

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

-

form

solution, suspension

form

suspension

form

ammonium sulfate suspension

form

lyophilized

application(s)

life science and biopharma

application(s)

life science and biopharma

application(s)

-

application(s)

-


Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

No data available

flash_point_c

No data available



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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)
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
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).



Global Trade Item Number

SKUGTIN
1012724800104061838667250
1012791400104061838667571
1012725600104061838667267