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10107085001

Roche

L-Lactate Dehydrogenase (L-LDH)

from hog muscle

Synonyme(s) :

L-LDH, L-Lactate Dehydrogenase, L-lactate

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About This Item

Numéro de classification (Commission des enzymes):
1.1.1.27 (BRENDA, IUBMB)
Code UNSPSC :
12352204

Source biologique

hog muscle

Niveau de qualité

100

Forme

suspension

Activité spécifique

~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.)

Conditionnement

pkg of 10 mL (100 mg)

Fabricant/nom de marque

Roche

Catégories apparentées

Description générale

L-Lactate Dehydrogenase (L-LDH) is an enzyme which is involved in the glycolytic pathway. It is believed to consist of five isotypes, LDH1 to LDH5. It also has a major role in carbohydrate metabolism of human malaria parasites.

Application

It was used in determination of D-Lactate.
Reduction of α-ketoacids to α-hydroxycarboxylic acids or reverse reaction.

Forme physique

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6.5

Autres remarques

For life science research only. Not for use in diagnostic procedures.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

does not flash

Point d'éclair (°C)

does not flash

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Consulter la Bibliothèque de documents

Thorsten Irsch et al.
The Journal of biological chemistry, 279(21), 22209-22217 (2004-02-21)
The glyoxalase system is a ubiquitous pathway catalyzing the glutathione-dependent detoxication of ketoaldehydes such as methylglyoxal, which is mainly formed as a by-product of glycolysis. The gene encoding a glyoxalase II has been cloned from Trypanosoma brucei, the causative agent
Plasmodium falciparum and Plasmodium vivax: Lactate-Dehydrogenase Activity and Its Application for in Vitro Drug Susceptibility Assay.
Basco, Leonardo K., et al.
Experimental Parasitology, 80.2, 260-271 (1995)
Mizeck Gg Chagunda et al.
The Journal of dairy research, 73(4), 431-440 (2006-07-11)
Systematic factors affecting the activities of L-lactate dehydrogenase (LDH) and N-acetyl-beta-D-glucosaminidase (NAGase) and somatic cell count (SCC), the association between the activities of LDH and NAGase and SCC with respect to udder health status, and the ability of LDH and
Heiko Henning et al.
Andrology, 10(7), 1426-1440 (2022-07-06)
Prolonging the shelf-life of liquid-preserved semen without compromising its fertilizing capacity may increase the efficiency of artificial insemination in pigs. Many fertilization-relevant processes are adenosine triphosphate dependent. The impact of semen storage and rewarming to body temperature on the energy

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