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L1254

Sigma-Aldrich

L-Lactic Dehydrogenase from rabbit muscle

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

Sinonimo/i:

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

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

rabbit muscle

Tipo

Type XI

Forma fisica

lyophilized powder

Attività specifica

600-1,200 units/mg protein

PM

140 kDa

Composizione

protein, 90-100%

Condizioni di stoccaggio

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

tecniche

activity assay: suitable

Colore

white

Attività estranea

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

Temperatura di conservazione

−20°C

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Descrizione generale

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 .

Applicazioni

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

Azioni biochim/fisiol

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.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Definizione di unità

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

Risultati analitici

Protein determined by biuret.

Anticorpo

Enzima

N° Catalogo
Descrizione
Determinazione del prezzo

Prodotti correlati

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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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
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
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
Farhana A and Lappin. SL
Biochemistry (2022)
Yicong Cai et al.
Plant biotechnology journal, 16(11), 1878-1891 (2018-03-27)
Starch is the main form of energy storage in higher plants. Although several enzymes and regulators of starch biosynthesis have been defined, the complete molecular machinery remains largely unknown. Screening for irregularities in endosperm formation in rice represents valuable prospect

Articoli

For use as a marker in SDS-PAGE; Albumin from chicken egg white, For use as a marker in SDS-PAGE; L-Lactic Dehydrogenase from rabbit muscle, Type XI, lyophilized powder, 600-1,200 units/mg protein

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