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Merck

L1006

Sigma-Aldrich

L-Lactic Dehydrogenase from bovine heart

Type XVII, buffered aqueous glycerol solution, ≥400 units/mg protein

Sinónimos:

Lactate, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine heart

type

Type XVII

assay

5.0—15.0 mg protein/mL (biuret)

form

buffered aqueous glycerol solution

specific activity

≥400 units/mg protein

mol wt

140 kDa

manufacturer/tradename

Sigma-Aldrich

technique(s)

cell based assay: suitable

impurities

<10 μg/mg protein free ammonium

color

white

pH

7.5

cation traces

NH4+: ≤10 μg/mg protein

UniProt accession no.

application(s)

life science and biopharma

foreign activity

glutamic-pyruvic transaminase and glutamic-oxalacetic transaminase ≤0.02%
pyruvate kinase, myokinase and α-glycerophosphate dehydrogenase ≤0.01%

storage temp.

2-8°C

Gene Information

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General description

Research area: Cell signaling. L-LacticDehydrogenase (LDH) is present in the cell cytoplasm. and is part of the glycolytic pathway. Lactate dehydrogenase (LDH) is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family. It has five isozymes (LD1 to LD5) and this composition varies in different tissues. LD1 is present at higher concentrations in the heart, kidneys, and erythrocytes. LD5 is found in the liver and skeletal muscles.(2)

Application

L-Lactic Dehydrogenase from bovine heart has been used in ATPase assay of R2 complex Rvb1p-Rvb2p, RecA protein and sarcoplasmic reticulum Ca2+-ATPase (SERCA).

Biochem/physiol Actions

Variation in the levels of L-Lactic Dehydrogenase (LDH) isoform is a diagnostic marker for tissue damage. The levels of LDH is useful in detecting dairy cattle disease, Mastitis. Dye based purified LDH from bovine heart has analytical applications.Lactic dehydrogenase (LDH)plays an essential role in the glycolytic pathway where it is involved in the conversionof pyruvate to lactate using NAD+as a co-factor. It is considered an important molecule that can be used incancer therapy as it acts as a glycolytic inhibitor. Inhibition of LDH isassociated with blocking of aerobic glycolysis in the tumour cells.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Unit Definition

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Physical form

Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5

Analysis Note

Protein determined by biuret

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1


Certificados de análisis (COA)

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Determination of lactate dehydrogenase (LDH) activity in milk by a fluorometric assay
Larsen T
The Journal of Dairy Research, 72(2), 209-216 (2005)
Simultaneous purification of L-malate dehydrogenase and L-lactate dehydrogenase from bovine heart by biomimetic-dye affinity chromatography
Labrou NE and Clonis YD
Bioprocess and Biosystems Engineering, 16(3), 157-161 (1997)
Purified E255L mutant SERCA1a and purified PfATP6 are sensitive to SERCA-type inhibitors but insensitive to artemisinins
Cardi D, et al.
The Journal of Biological Chemistry, 285(34), 26406-26416 (2010)
Active displacement of RecA filaments by UvrD translocase activity
Petrova V, et al.
Nucleic Acids Research, 43(8), 4133-4149 (2015)
Ligand binding and protein dynamics in lactate dehydrogenase
Pineda JR, et al.
Biophysical Journal, 93(5), 1474-1483 (2007)

Protocolos

This procedure applies to all products from heart muscle that have a specification for L-Lactic Dehydrogenase activity.

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