M1567
Malic Dehydrogenase from porcine heart
≥600 units/mg protein (biuret), ammonium sulfate suspension
Sinónimos:
L-Malate: NAD+ oxidoreductase, MDH, Malate Dehydrogenase
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UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-622-5
MDL number:
Specific activity:
≥600 units/mg protein (biuret)
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Permítanos ayudarleform
ammonium sulfate suspension
specific activity
≥600 units/mg protein (biuret)
foreign activity
Glutamic-Oxalacetic Transaminase ≤0.01%, Glutamic-Pyruvic Transaminase ≤0.01%
storage temp.
2-8°C
Quality Level
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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.
Physical form
Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0
Other Notes
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.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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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