10107085001
Roche
L-Lactate Dehydrogenase (L-LDH)
from hog muscle
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biological source
hog muscle
Quality Level
form
suspension
specific activity
~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.)
packaging
pkg of 10 mL (100 mg)
manufacturer/tradename
Roche
Related Categories
General description
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.
Physical form
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6.5
Other Notes
For life science research only. Not for use in diagnostic procedures.
WGK
WGK 1
Flash Point(F)
does not flash
Flash Point(C)
does not flash
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
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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
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)
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
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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