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Merck

L1254

L-Lactic Dehydrogenase from rabbit muscle

Type XI, lyophilized powder, 600-1,200 units/mg protein

Synonyme(s) :

Anaerobic Lactate Dehydrogenase, Lactate, NAD-lactate dehydrogenase, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD

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A propos de cet article

Numéro CAS:
9001-60-9
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-617-8
MDL number:
MFCD00131466
Numéro CE :
1.1.1.27 (BRENDA, IUBMB)
Specific activity:
600-1,200 units/mg protein
Biological source:
rabbit muscle

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Nom du produit

L-Lactic Dehydrogenase from rabbit muscle, Type XI, lyophilized powder, 600-1,200 units/mg protein

biological source

rabbit muscle

type

Type XI

form

lyophilized powder

specific activity

600-1,200 units/mg protein

mol wt

140 kDa

composition

protein, 90-100%

storage condition

(Keep container tightly closed in a dry and well-ventilated place)

technique(s)

activity assay: suitable

color

white

foreign activity

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

storage temp.

−20°C

Quality Level

200

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Analysis Note

Protein determined by biuret.

Application

L-Lactic Dehydrogenase from rabbit muscle has been used:
  • as a component of activation and relaxing solution in ATPase activity and isometric steady-state tension measurements with muscle fiber
  • in Trypanosoma congolense pyruvate kinase activity assay
  • in pyruvate kinase (PK) assay with rice plastidic PK enzyme OsPK2

Biochem/physiol Actions

Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
Muscle-type Lactic Dehydrogenase (LDH) participates in metabolic pathways and its activity is essential for anaerobic glycolysis. LDH activity is inhibited by ascorbate. LDH regenerates nicotinamide adenine dinucleotide (NAD+) from NADH and is industrially useful in poly(lactic acid) production. In the absence of oxygen, LDH participates in a fermentation reaction, catalyzes pyruvate into lactic acid, and oxidizes nicotinamide adenine dinucleotide (NADH) to NAD+. Therefore, LDH mediates the production of NAD+ essential anaerobic glycolysis pathway. Through this LDH helps maintain the physiological and biochemical functions of the cell in the absence of oxygen.

General description

Research area: Cell Signaling
Lactic Dehydrogenase (LDH) has a total molecular weight of 140 kDa and is composed of 4 subunits which are designated M subunit (muscle) and H subunit (heart). These subunits may be mixed in any of 5 combinations (M4, M3H1, M2H2, MH3, and H4). Skeletal muscle contains LDH that is predominately M4 with some small amounts of M3H and traces of H2H2. The H and M subunits are quite similar in molecular weight, but differ substantially in amino acid composition. Rabbit muscle LDH dissociates into dimeric species (MW = ~70 kDa) in acetate-chloride at pH 5.0, the dissociation is reversible. Biochemistry, 13, 3527-3531 (1974). Oxidizes glyoxylate and lactate.
Isoelectric point: 8.4-8.6
Optimal pH : 7.5 .

Other Notes

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000504666
0000504665
0000504665
0000504666
0000492598

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Consulter la Bibliothèque de documents

Belén Torrado et al.
Biomedical optics express, 12(7), 3760-3774 (2021-08-31)
We describe a method based on a pair of transmission filters placed in the emission path of a microscope to resolve the emission wavelength of every point in an image. The method can be applied to any type of imaging
Farhana A and Lappin. SL
Biochemistry (2022)
John Jeshurun Michael et al.
Journal of the American Heart Association, 5(3), e002777-e002777 (2016-03-24)
We hypothesized that the functional effects of R206L-a rat analog of the dilated cardiomyopathy (DCM) mutation R205L in human cardiac troponin T (TnT)-were differently modulated by myosin heavy chain (MHC) isoforms and T204E, a protein kinase C (PKC) phosphomimic of
Matthew Warren Eggert et al.
Applied biochemistry and biotechnology, 165(2), 676-686 (2011-06-01)
In order to evaluate the effectiveness of L: -lactate dehydrogenase (LDH) from rabbit muscle as a regenerative catalyst of the biologically important cofactor nicotinamide adenine dinucleotide (NAD), the kinetics over broad concentrations were studied to develop a suitable kinetic rate
Percy J Russell et al.
Journal of enzyme inhibition and medicinal chemistry, 19(1), 91-98 (2004-06-19)
Muscle-type LDH (LDH-m4) activity is critical for efficient anaerobic glycolysis. The results here show that rabbit LDH-M4 is inhibited by concentrations of ascorbate normally found in tissues. Aldolase and muscle G-actin were found to protect and to reverse inhibitions of
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