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M9004

Sigma-Aldrich

Malic Dehydrogenase from bovine heart

ammonium sulfate suspension, 2000-4000 units/mg protein (modified Warburg-Christian)

Sinónimos:

L-Malate:NAD+ oxidoreductase, MDH

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About This Item

Comisión internacional de enzimas:
1.1.1.37 (BRENDA, IUBMB)
EC Number:
232-622-5
MDL number:
MFCD00131567
UNSPSC Code:
12352204
NACRES:
NA.54
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biological source

bovine heart

Quality Level

200

form

ammonium sulfate suspension

specific activity

2000-4000 units/mg protein (modified Warburg-Christian)

mol wt

35 kDa

impurities

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

storage temp.

2-8°C

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General description

Malic Dehydrogenase from bovine heart contains a histidine residue at the NAD-binding active site which is critical for activity. When this histidine is mutated a loss in activity is observed. [1]
Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.

Application

Malic dehydrogenase has been used in a study to assess a flow injection system for on-line monitoring of fumaric acid in biological processes. [2] It has also been used in a study to investigate a root-knot nematode parasitizing peanut in Texas. [3]

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 3 M (NH4)2SO4 - 0.01 M KH2PO4 solution, pH 7.3

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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Certificados de análisis (COA)

Lot/Batch Number
0000310632
0000310632
0000287282
0000280687
0000265932

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Z Y Chen et al.
Plant physiology, 112(2), 677-684 (1996-10-01)
At low-CO2 (air) conditions, the unicellular green alga Chlamydomonas reinhardtii acquires the ability to raise its internal inorganic carbon concentration. To study this adaptation to low CO2, cDNA clones induced under low-CO2 growth conditions were selected through differential screening. One
J D Eisenback et al.
Journal of nematology, 35(4), 395-403 (2003-12-01)
Meloidogyne haplanaria n. sp. is described and illustrated from specimens parasitizing peanut in Texas. The perineal pattern of the female is rounded to oval with a dorsal arch that is high and rounded except for striae near the vulva, which
Isoelectric points and molecular weights of proteins: a new table.
Righetti, P.G., and Tudor, G.
Journal of Chromatography A, 220, 115-194 (1981)
Flow injection system for on-line monitoring of fumaric acid in biological processes
Rhee, J.
Analytica Chimica Acta, 499, 71-80 (2003)
E M Gregory
The Journal of biological chemistry, 250(14), 5470-5474 (1975-07-25)
Bovine mitochondrial malate dehydrogenase (EC 1.1.1.37) was inactivated by the specific modifications of a single histidine residue upon reaction with iodoacetamide. NADH protected against this loss of activity and reaction with the histidine residue, suggesting that the histidine is at
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Artículos

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocolos

Enzymatic Assay of Malic Dehydrogenase

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

Enzymatic Assay of Malic Dehydrogenase

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

Enzymatic Assay of Malic Dehydrogenase

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

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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