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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369.00 CHF
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1 080.00 CHF
About This Item
Produits recommandés
Source biologique
rabbit muscle
Niveau de qualité
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
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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 .
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]
Actions biochimiques/physiologiques
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.
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.
Anticorps
Enzyme
Réf. du produit
Description
Tarif
Inhibiteur
Réf. du produit
Description
Tarif
Produit(s) apparenté(s)
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
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)
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Certificats d'analyse (COA)
Lot/Batch Number
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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
Percy J Russell et al.
Journal of enzyme inhibition and medicinal chemistry, 19(1), 91-98 (2004-06-19)
Muscle-type LDH (LDH-m4) activity is critical for efficient anaerobic glycolysis. The results here show that rabbit LDH-M4 is inhibited by concentrations of ascorbate normally found in tissues. Aldolase and muscle G-actin were found to protect and to reverse inhibitions of
Articles
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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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-
Helpful?
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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.
Helpful?
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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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