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Merck

M1567

Sigma-Aldrich

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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About This Item

Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulario

ammonium sulfate suspension

Nivel de calidad

actividad específica

≥600 units/mg protein (biuret)

actividad extraña

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

temp. de almacenamiento

2-8°C

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Descripción general

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.

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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.

Forma física

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

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Visite la Librería de documentos

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)
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)
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

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocolos

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

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

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

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

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