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
• Numéro CAS: 9001-60-9
• Numéro de classification (Commission des enzymes): 1.1.1.27 (BRENDA, IUBMB)
• Numéro CE : 232-617-8
• Numéro MDL: MFCD00131466
• Code UNSPSC : 12352204
• Nomenclature NACRES : NA.54

Propriétés

• Source biologique: rabbit muscle
• Niveau de qualité: 200
• Type: Type XI
• Forme: lyophilized powder
• Activité spécifique: 600-1,200 units/mg protein
• Poids mol.: 140 kDa
• Composition: protein, 90-100%
• Conditions de stockage: (Keep container tightly closed in a dry and well-ventilated place)
• Technique(s): activity assay: suitable
• Couleur: white
• Activité étrangère: pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
• Température de stockage: −20°C

Description

Description générale

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 .

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Remarque sur l'analyse

Protein determined by biuret.

Informations sur la sécurité

• Pictogrammes: GHS08
• Mention d'avertissement: Danger
• Mentions de danger: H334
• Conseils de prudence: P261 - P284 - P501
• Classification des risques: Resp. Sens. 1
• Code de la classe de stockage: 11 - Combustible Solids
• Classe de danger pour l'eau (WGK): WGK 1
• Équipement de protection individuelle: Eyeshields, Gloves, type N95 (US)