L1254

L-Lactic Dehydrogenase from rabbit muscle

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

• Synonim(y): Anaerobic Lactate Dehydrogenase, Lactate, NAD-lactate dehydrogenase, (S)-Lactate: NAD⁺ oxidoreductase, L-LDH, LAD, LD
• Numer CAS: 9001-60-9
• UNSPSC Code: 12352204
• NACRES: NA.54
• EC Number: 232-617-8
• MDL number: MFCD00131466
• Numer WE: 1.1.1.27 (BRENDA, IUBMB)
• Specific activity: 600-1,200 units/mg protein
• Biological source: rabbit muscle

Właściwości

• biological source: rabbit muscle
• Quality Segment: 200
• 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

Opis

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 .

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[1]
• in Trypanosoma congolense pyruvate kinase activity assay[2]
• in pyruvate kinase (PK) assay with rice plastidic PK enzyme OsPK2[3]

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.[4] 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.

Analysis Note

Protein determined by biuret.

Other Notes

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

Ta strona może zawierać tekst przetłumaczony maszynowo.

Informacja o środkach bezpieczeństwa

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Klasa składowania: 11 - Combustible Solids
• wgk: WGK 1
• ppe: Eyeshields, Gloves, type N95 (US)