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LMDH-RO

Roche

L-Malate Dehydrogenase (L-MDH)

from pig heart (mitochondrial)

Synonym(s):
L-MDH
Enzyme Commission number:

Quality Level

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

optimum pH

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

shipped in

wet ice

storage temp.

2-8°C

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This Item
LLDH-RO442610-M10107085001
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

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

specific activity

~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.)

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Roche

optimum pH

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

optimum pH

-

optimum pH

-

optimum pH

-

shipped in

wet ice

shipped in

wet ice

shipped in

-

shipped in

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

-

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.

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.

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.

Quality

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

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+

Other Notes

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

No data available

Flash Point(C)

No data available


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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).

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