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P0294

Sigma-Aldrich

Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle

For the Determination of ADP, buffered aqueous glycerol solution

Sinónimos:

PK/LDH enzymes from rabbit muscle

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5 ML
MXP 5,018.00
5 X 5 ML
MXP 18,854.00

MXP 5,018.00


Disponible para envío el31 de marzo de 2025Detalles


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5 ML
MXP 5,018.00
5 X 5 ML
MXP 18,854.00

About This Item

Código UNSPSC:
12352204
NACRES:
NA.54

MXP 5,018.00


Disponible para envío el31 de marzo de 2025Detalles


Solicitar un pedido a granel

Formulario

buffered aqueous glycerol solution

mol peso

59 kDa

concentración

600-1,000 units/mL pyruvate kinase
900-1400 units/mL lactic dehydrogenase

temp. de almacenamiento

−20°C

Descripción general

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]

Aplicación

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]

Acciones bioquímicas o fisiológicas

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]

Definición de unidad

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.

Forma física

Solution in 50% glycerol containing 10 mM HEPES, pH 7.0, 100 mM KCl and 0.1 mM EDTA

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Spontaneous motion in hierarchically assembled active matter
Sanchez T, et al.
Nature, 491(7424), 431-431 (2012)
Pazit Shaul et al.
Organic & biomolecular chemistry, 9(11), 4057-4063 (2011-03-03)
Amongst the many synthetic aminoglycoside analogues that were developed to regain the efficacy of this class of antibiotics against resistant bacterial strains, the 1-N-acylated analogues are the most clinically used. In this study we demonstrate that 6'-N-acylation of the clinically
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)
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)

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