P0294
Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle
For the Determination of ADP, buffered aqueous glycerol solution
Synonyme(s) :
PK/LDH enzymes from rabbit muscle
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5 ML
207,00 €
5 X 5 ML
717,00 €
About This Item
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Niveau de qualité
Forme
buffered aqueous glycerol solution
Poids mol.
59 kDa
Concentration
600-1,000 units/mL pyruvate kinase
900-1400 units/mL lactic dehydrogenase
Température de stockage
−20°C
Description générale
Pyruvate Kinase from rabbit muscle is a metalloenzyme which catalyzes the conversion of phosphoenol pyruvate to pyruvate in the glycolysis pathway. It corresponds to a molecular weight of 59 kDa.[1] It exists as a tetramer and undergoes conformational changes in the active site to accommodate substrate.[2] Lactic dehydrogenase (LDH) catalyzes the lactate to pyruvate conversion in anaerobic glycolysis. It exists as tetramer and comprises of two subunits (H and M).[3] The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality.[4]
Application
Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle has been used:
- for ATP generation in the active microtubule preparation[5]
- in the enzyme linked ATPase assay of skeletal muscle heavy meromyosin (HMM)[6]
- as a standard control for quantifying mesenchymal stem cells (MSCs) lactate dehydrogenase[7]
Actions biochimiques/physiologiques
ADP Quantification Assay protocol for the use of PK/LDH in the determination of ADP. Solutions containing unkown concentrations of ADP can be substuted for reagent D in this protocol. Further dilutions of the ADP solution may be required
Lactate dehydrogenase from rabbit muscle can be inhibited by ascorbate. Aldolase and actin were shown to block this inhibitory effect. [8]
Pyruvate kinase also catalyzes the phosphorylation of thiamine diphosphate (TDP) to thiamine triphosphate (TTP) which may find application in antiviral and tumor therapy.[1]
Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur. [9]
Définition de l'unité
Pyruvate kinase activity: One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C.
Lactic dehydrogenase activity: One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Lactic dehydrogenase activity: One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Forme physique
Solution in 50% glycerol containing 10 mM HEPES, pH 7.0, 100 mM KCl and 0.1 mM EDTA
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Les clients ont également consulté
Cai-Hong Yun et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(6), 2070-2075 (2008-01-30)
Lung cancers caused by activating mutations in the epidermal growth factor receptor (EGFR) are initially responsive to small molecule tyrosine kinase inhibitors (TKIs), but the efficacy of these agents is often limited because of the emergence of drug resistance conferred
Ligand-Induced Domain Movement in Pyruvate Kinase: Structure of the Enzyme from Rabbit Muscle with Mg2+, K+, and l-Phospholactate at 2.7 AA Resolution
Larsen TM, et al.
Archives of Biochemistry and Biophysics, 345(2), 199-206 (1997)
Jianming Zhang et al.
Nature, 463(7280), 501-506 (2010-01-15)
In an effort to find new pharmacological modalities to overcome resistance to ATP-binding-site inhibitors of Bcr-Abl, we recently reported the discovery of GNF-2, a selective allosteric Bcr-Abl inhibitor. Here, using solution NMR, X-ray crystallography, mutagenesis and hydrogen exchange mass spectrometry
Thermal activation of `allosteric-like?large-scale motions in a eukaryotic Lactate Dehydrogenase
Katava M, et al.
Scientific Reports, 7, 41092-41092 (2017)
Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase
Boehme C, et al.
Biological Chemistry, 394(5), 695-701 (2013)
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