L1254
L-Lactic Dehydrogenase from rabbit muscle
Type XI, lyophilized powder, 600-1,200 units/mg protein
Synonym(s):
Anaerobic Lactate Dehydrogenase, Lactate, NAD-lactate dehydrogenase, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD
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About This Item
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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
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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 .
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
Biochem/physiol Actions
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.
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Analysis Note
Protein determined by biuret.
antibody
enzyme
Product No.
Description
Pricing
inhibitor
Product No.
Description
Pricing
related product
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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