Malate Dehydrogenase from Porcine Heart Mitochondria

Description

Malate Dehydrogenase from Porcine Heart Mitochondria

Malate Dehydrogenase (MDH) from porcine heart mitochondria is a key enzyme in the citric acid cycle, catalyzing the reversible oxidation of malate to oxaloacetate using NAD as a coenzyme. This highly purified preparation is supplied as a lyophilized powder with an activity range of 50100 U/mg solid, making it suitable for a wide range of biochemical and metabolic studies.

MDH plays a central role in cellular respiration and energy production, and is frequently used in enzyme kinetics, mitochondrial function assays, and redox biology. This product is stable at 20C and should be reconstituted in sterile buffer for optimal performance. All components are prepared using Type I ultrapure water and filtered through 0.22 m membranes to ensure consistency and reproducibility across batches.

Key benefits:

• High-purity mitochondrial MDH from porcine heart
• Validated activity range (50100 U/mg solid)
• Lyophilized format for long-term stability
• Supports metabolic, enzymatic, and redox research
• Ideal for citric acid cycle and NAD/NADH studies

Indication for Use:
This product is for Research Use Only (RUO). It is not intended for human or animal use, diagnostic procedures, or therapeutic applications.

References:

• Gleason WB et al. Refined crystal structure of MDH. Biochemistry. 1994;33(8):207888.
• Roderick SL et al. 3D structure of MDH. J Biol Chem. 1986;261(20):94614.
• Eberhardt NL et al. CD spectra of MDH complexes. J Biol Chem. 1975;250(8):298792.
• Fernley RT et al. MDH isolation and comparison. Biosci Rep. 1981;1(6):497507.
• Schindler PW. Chlorothricin inhibition of MDH isoenzymes. Eur J Biochem. 1975;51(2):57985.
• Roderick SL et al. MDH conformation via electron density. J Biol Chem. 1983;258(19):1163642.
• Shore JD et al. NADH binding to MDH. J Biol Chem. 1979;254(18):905962.
• Grant PM et al. Precursor vs mature MDH forms. Biochemistry. 1987;26(1):12834.
• Fahien LA et al. GLDHMDH complex. Arch Biochem Biophys. 1979;192(1):3346.
• Wimmer MJ et al. Biphasic inactivation of MDH by pyridoxal 5-phosphate. J Biol Chem. 1975;250(2):7105.