M7032
Malic Dehydrogenase from Thermus flavus
lyophilized powder, ≥50 units/mg solid
Synonym(s):
L-Malate: NAD+ oxidoreductase, MDH
form
lyophilized powder
specific activity
≥50 units/mg solid
storage temp.
−20°C
General description
Malic dehydrogenase from Thermus flavus is stable and active at 90 ° C.
Application
Malic dehydrogenase has been used in a study to assess electron transport chain activity in mitochondria from human skeletal muscle. It has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia.
Physical form
Contains dextran
Other Notes
One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25 °C.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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C A Kelly et al.
Biochemistry, 32(15), 3913-3922 (1993-04-20)
A binary complex of malate dehydrogenase from the thermophilic bacterium Thermus flavus (tMDH) with NADH has been crystallized from poly(ethylene glycol) 3500, pH 8.5, yielding diffraction-quality crystals in space group P2(1)2(1)2(1). The structure was solved at 1.9-A resolution using molecular
Ewa Grucka-Mamczar et al.
Annales Academiae Medicae Stetinensis, 50 Suppl 1, 36-41 (2006-08-09)
The study was done in 30 one-month-old Wistar FL rats divided into one control and two study groups of ten animals each. Hyperglycemia was induced with sodium fluoride in water at a concentration of 50 or 100 mg/L during four
G Ferreira et al.
Journal of dairy science, 90(3), 1460-1466 (2007-02-14)
Biotin is a cofactor of the gluconeogenic enzymes pyruvate carboxylase (PC) and propionyl-coenzyme A carboxylase (PCC). We hypothesized that biotin supplementation increases the activity and gene expression of PC and PCC and the gene expression of phosphoenol-pyruvate carboxykinase (PEPCK) in
Vladimir B Ritov et al.
Analytical biochemistry, 333(1), 27-38 (2004-09-08)
This study addresses an application of pyridine nucleotide enzymatic analyses to evaluate the activity of the mitochondrial electron transport chain (reduced nicotinamide adenine dinucleotide (NADH) oxidase) and Complexes I and II in samples of human muscle as small as approximately
Seung-Min Lee et al.
Biogerontology, 13(5), 525-536 (2012-09-14)
Carbohydrate metabolism changes during cellular senescence. Cytosolic malate dehydrogenase (MDH1) catalyzes the reversible reduction of oxaloacetate to malate at the expense of reduced nicotinamide adenine dinucleotide (NADH). Here, we show that MDH1 plays a critical role in the cellular senescence
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