P0294
Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle
For the Determination of ADP, buffered aqueous glycerol solution
Sinonimo/i:
PK/LDH enzymes from rabbit muscle
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About This Item
Codice UNSPSC:
12352204
NACRES:
NA.54
Prodotti consigliati
Forma fisica
buffered aqueous glycerol solution
PM
59 kDa
Concentrazione
600-1,000 units/mL pyruvate kinase
900-1400 units/mL lactic dehydrogenase
Temperatura di conservazione
−20°C
Descrizione generale
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. It exists as a tetramer and undergoes conformational changes in the active site to accommodate substrate. Lactic dehydrogenase (LDH) catalyzes the lactate to pyruvate conversion in anaerobic glycolysis. It exists as tetramer and comprises of two subunits (H and M). The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality.
Applicazioni
Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle has been used:
- for ATP generation in the active microtubule preparation
- in the enzyme linked ATPase assay of skeletal muscle heavy meromyosin (HMM)
- as a standard control for quantifying mesenchymal stem cells (MSCs) lactate dehydrogenase
Azioni biochim/fisiol
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.
Pyruvate kinase also catalyzes the phosphorylation of thiamine diphosphate (TDP) to thiamine triphosphate (TTP) which may find application in antiviral and tumor therapy.
Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur.
Definizione di unità
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.
Stato fisico
Solution in 50% glycerol containing 10 mM HEPES, pH 7.0, 100 mM KCl and 0.1 mM EDTA
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 2
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificati d'analisi (COA)
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I clienti hanno visto anche
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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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)
Keith D Green et al.
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S Ainsworth et al.
The Biochemical journal, 145(1), 63-71 (1975-01-01)
The paper reports a comparative study of the effects of Mn2+, Ni2+ and Co2+ on the reaction of ADP with phosphoenolypyruvate when catalysed by K+-activated rabbit muscle pyruvate kinase. The activation and subsequent inhibition that occurs as the bivalent ion
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