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M1567

Sigma-Aldrich

Malic Dehydrogenase from porcine heart

≥600 units/mg protein (biuret), ammonium sulfate suspension

Synonym(s):

L-Malate: NAD+ oxidoreductase, MDH, Malate Dehydrogenase

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About This Item

Enzyme Commission number:
1.1.1.37 (BRENDA, IUBMB)
EC Number:
232-622-5
MDL number:
MFCD00131567
UNSPSC Code:
12352204
NACRES:
NA.54

form

ammonium sulfate suspension

Quality Level

200

specific activity

≥600 units/mg protein (biuret)

foreign activity

Glutamic-Oxalacetic Transaminase ≤0.01%
Glutamic-Pyruvic Transaminase ≤0.01%

storage temp.

2-8°C

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General description

Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.
Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity.
Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.

Application

Malic Dehydrogenase from porcine heart has been used:
  • in qualitative protein binding measurements
  • to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair
  • to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase

Malic dehydrogenase has been used in a study to assess the effect of an immunomodulator S2 complex on the enzymes of the parasites. It has also been used in a study to investigate the heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid.

Biochem/physiol Actions

Malic Dehydrogenase (MDH) plays an important role in the citric acid cycle in mitochondria. It catalyzes the interconversion of substrates malate and oxaloacetate with the simultaneous oxidation/reduction of NAD/NADH+. MDH present in the cytosol is involved in the shuttling of malate/aspartate.

Unit Definition

One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25°C.

Physical form

Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Electrochemical Coupled-Enzyme Assays at Carbon Nanotubes
Zhang M, et al.
Analytical Chemistry, 86(18), 9330-9334 (2014)
Heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid
Lowenthal, A., et al.
Journal of Neurochemistry, 7, 135-140 (2006)
Malate dehydrogenases-structure and function
Minarik P, et al.
General Physiology and Biophysics, 21(3), 257-266 (2002)
Sensing NADH conformation using phasor analysis on fluorescence spectra
Palo D, et al.
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 186(3), 105-111 (2017)
Sandip K Nandi et al.
Biochemical and biophysical research communications, 533(4), 1352-1358 (2020-10-22)
The chaperone activity of α-crystallin is important for maintaining the transparency of the human lens. αB-crystallin (αBC) is a long-lived protein in the lens that accumulates chemical modifications during aging. The formation of advanced glycation end products (AGEs) through glycation
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Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

Enzymatic Assay of Malic Dehydrogenase

Spectrophotometric assay evaluates malic dehydrogenase activity using bovine heart enzyme with critical histidine residue at active site.

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