In this assay, the activity of L-Lactic Dehydrogenase is determined by observing the decrease in absorbance at 340 nm for NADH, rather than the formation of NAD+. The method utilizes a continuous spectrophotometric rate determination to monitor the absorbance decrease at 340 nm, corresponding to NADH absorbance.
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-617-8
MDL number:
Numéro CE :
Specific activity:
600-1,200 units/mg protein
Biological source:
rabbit muscle
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rabbit muscle
Quality Segment
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
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.
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.
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Cet article | |||
|---|---|---|---|
| description Type XI, lyophilized powder, 600-1,200 units/mg protein | description Type II, ammonium sulfate suspension, 800-1,200 units/mg protein | description Type X, ammonium sulfate suspension, ≥600 units/mg protein | description 1000 units/mL |
| biological source rabbit muscle | biological source - | biological source bovine muscle | biological source - |
| specific activity 600-1,200 units/mg protein | specific activity 800-1,200 units/mg protein | specific activity ≥600 units/mg protein | specific activity 1000 units/mL |
| technique(s) activity assay: suitable | technique(s) - | technique(s) activity assay: suitable | technique(s) - |
| form lyophilized powder | form ammonium sulfate suspension | form ammonium sulfate suspension | form solution |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| mol wt 140 kDa | mol wt 140 kDa | mol wt - | mol wt - |
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Mot-clé
Danger
Codes de danger
Mentions de précaution
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
WGK
WGK 1
EPI (équipement de protection individuelle)
Eyeshields, Gloves, type N95 (US)
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In the assay, the UV-Vis absorbance at 340 nm is always showing negative. If lactate continues to form over time, shouldn't the absorbance become more positive?
1 answer-
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What are products that only have the quality release date on the COA and do not have an expiration or retest date?
1 answer-
Certain products are not included in the retest or expiration date programs as there is no indication to suggest that they are unstable. These products will only display the Release Date on the certificate of analysis, with no stated Retest, Expiration, or Use-by Date. It is advised to handle these products according to the defined conditions outlined in our product literature and website product descriptions. It is recommended for end users to regularly inspect these products to ensure they perform as expected. For such products, our standard warranty of 1 year from the date of shipment applies. For more information on our warranty, please refer to the terms and conditions of sale.
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is the substrate given for the enzyme lactate or lactic form, and may I know why it is L-lactic dehydrogenase and not L-lactate dehydrogenase?
1 answer-
The terms tend to be used interchangeably. Lactate is the anion of the conjugate base lactic acid.
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/216/153/l1254enz.pdfHelpful?
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