M1567
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
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form
ammonium sulfate suspension
Quality Level
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)
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Experimental parasitology, 112(2), 85-91 (2005-11-09)
S(2) complex has been reported to have a direct antileishmanial effect. The possibility that the direct antileishmanial effect may be due to inhibition of key enzymes involved in glucose metabolism and/ or enzymes associated with virulence was investigated. Cell pellets
Heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid
Journal of Neurochemistry, 7, 135-140 (2006)
Electrochemical Coupled-Enzyme Assays at Carbon Nanotubes
Analytical Chemistry, 86(18), 9330-9334 (2014)
Malate dehydrogenases-structure and function
General Physiology and Biophysics, 21(3), 257-266 (2002)
Sensing NADH conformation using phasor analysis on fluorescence spectra
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 186(3), 105-111 (2017)
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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