Merck

LLDH-RO

Roche

L-Lactate Dehydrogenase (L-LDH)

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Comisión internacional de enzimas:

biological source

rabbit muscle

Quality Level

form

suspension

specific activity

~550 units/mg protein (at 25 °C (1,100 U/mg at 37 °C) with pyruvate as the substrate.)

mol wt

140,000  Da

packaging

pkg of 10 mL (10127884001 [100 mg])
pkg of 2 mL (10127230001 [10 mg])
pkg of 5 mL (10127876001 [25 mg])

manufacturer/tradename

Roche

technique(s)

activity assay: suitable

color

white

pH

6.0-7.0

solubility

water: miscible

NCBI accession no.

UniProt accession no.

application(s)

life science and biopharma

foreign activity

Aldolase <0.001%
GOT <0.01%
GPT <0.01%
MDH <0.01%
PK <0.001%
myokinase <0.01%

shipped in

wet ice

storage temp.

2-8°C

Gene Information

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Este artículo
LMDH-RO10107085001L3916
L-Lactate Dehydrogenase (L-LDH)

LLDH-RO

L-Lactate Dehydrogenase (L-LDH)

L-Malate Dehydrogenase (L-MDH) from pig heart (mitochondrial)

LMDH-RO

L-Malate Dehydrogenase (L-MDH)

specific activity

~550 units/mg protein (at 25 °C (1,100 U/mg at 37 °C) with pyruvate as the substrate.)

specific activity

~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.)

specific activity

~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.)

specific activity

1000 units/mL

Gene Information

rabbit ... LOC100355262(100355262)

Gene Information

Porcine ... MDH2(397039)

Gene Information

-

Gene Information

-

biological source

rabbit muscle

biological source

Porcine heart (mitochondrial)

biological source

hog muscle

biological source

-

form

suspension

form

solution, suspension

form

suspension

form

solution

application(s)

life science and biopharma

application(s)

life science and biopharma

application(s)

-

application(s)

-

General description

L-lactate:NAD+ oxidoreductase.
L-lactate dehydrogenase catalyzes the reversible reduction of pyruvate to L-lactate.

Specificity

L()-Lactate dehydrogenase (LDH) is specific for L()-lactate (relative rate = 100). It does not react with D(-)-lactate.LDH will also slowly oxidize glyoxylate (oxoacetate), glycerate and 3-halogen derivatives of L-lactate (rate with each, ≤ 1); 3-phosphoglycerate does not react.LDH will reduce pyruvate (2-oxopropanate; relative rate = 100) and other 2-oxoacids (e.g., 2-oxobutyrate), with rates decreasing rapidly with increasing chain length of the acid. Heart LDH reacts with 2-oxobutyrate at a greater rate than does skeletal muscle LDH.LDH will also oxidize 2,4-diketoacids (relative rate = 10). The enzyme is realtively specific for NAD(H) (relative rate = 100); NADP(H) is utilized much less efficiently (relative rate < 1). Representative Kms for (hog) skeletal muscle LDH (pH 7.5) are lactate, 8.3 mM; pyruvate, 0.12 mM; NAD, 0.10 mM; NADH, 0.012 mM.Representative Kms for (pig) heart LDH (pH 7.5) are lactate, 3.3 mM; pyruvate, 0.15 mM; NAD, 0.07 mM;NADH, 0.011 mM. In general, the concentration of pyruvate (reduction reaction) or of L-lactate (oxidation reaction) necessary to obtain a maximal rate with LDH is lower for preparations from heart tissue than for the preparations from skeletal muscle.

Application

Reduction of α-ketoacids to α-hydroxycarboxylic acids, or reverse reaction.

Sequence

LDH is a tetramer (MW = approx. 140,000 D, rabbit muscle or pig heart LDH). In mammals, there are two types of LDH subunits, M and H, with similar molecular weight (subunit MW ≈ 36,500 D) but differing amino acid composition.
Therefore, 5 electrophoretically distinguishable LDH isoenzymes, LDH-1 through LDH-5, of differing subunit composition, are found in mammals.
The molecular weight of all LDH isoenzymes is approximately the same.
– LDH-1 (H4), LDH-2 (H3M): predominant components of heart LDH
– LDH-3 (H2M2): principal component of LDH from lymphatic tissue
– LDH-4 (HM3), LDH-5 (M4): predominate in skeletal muscle or liver LDH

Note: The M subunit of LDH used to be designated the A subunit; the H subunit was the B subunit. Under the old designation, LDH-1 isoenzyme was LDH-B4.

Unit Definition

One unit (U) lactate dehydrogenase will reduce 1 µmol of pyruvate to L-lactate in 1 minute at +25 °C and pH 7.0.







Note: For preparations H and I, the activity is defined at +30 °C, pH 7.8. The above assay consumes 1 mol of NADH per mol of pyruvate reduced.





Unit Conversion: For the reduction reaction, pyruvate as substrate:





1 U (+25 °C) 1.5 U (+37 °C) [hog muscle LDH in glycerol].





1 U (+25 °C) 1.8 U (+37 °C) [hog muscle LDH in amm onium sulfate].





1 U (+25 °C) 1.1 U (+30 °C) 2.0 U (+37 °C) [rabbit muscle LDH].





1 U (+25 °C) 1.4 U(+30 °C) 2.5 U (+37 °C) [pig heart LDH].





1 U (+25 °C) 2.5 U (+37 °C) [beef heart LDH].

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 7

Preparation Note

Activator: 2-amino-2-methyl-1-propanol, diethanolamine, fluoride and heparin (oxidation reaction). Sodium sulfite (Na2SO3) will protect the enzyme from the effects of thiol-attacking reagents. Mercaptans can reverse the inhibitory effects of thiol-attacking reagents.

Analysis Note

Absorbance:The purified enzyme from beef heart has an absorbance of 14.9 (10 mg/ml, 280 nm).

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


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L-Lactate dehydrogenase: substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
Kim Mahn Joo
Journal of the American Chemical Society, 110.9, 2959-2964 (1988)
Agata M Pudlik et al.
Journal of bacteriology, 193(3), 706-714 (2010-12-01)
Carbohydrate/citrate cometabolism in Lactococcus lactis results in the formation of the flavor compound acetoin. Resting cells of strain IL1403(pFL3) rapidly consumed citrate while producing acetoin when substoichiometric concentrations of glucose or l-lactate were present. A proton motive force was generated
Enrico Desideri et al.
Autophagy, 10(9), 1652-1665 (2014-07-22)
Increased glycolytic flux is a common feature of many cancer cells, which have adapted their metabolism to maximize glucose incorporation and catabolism to generate ATP and substrates for biosynthetic reactions. Indeed, glycolysis allows a rapid production of ATP and provides

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