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P0294

Sigma-Aldrich

Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle

For the Determination of ADP, buffered aqueous glycerol solution

Szinonimák:

PK/LDH enzymes from rabbit muscle

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352204
NACRES:
NA.54

Minőségi szint

form

buffered aqueous glycerol solution

molekulatömeg

59 kDa

koncentráció

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

tárolási hőmérséklet

−20°C

Általános leírás

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.

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Egység definíció

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.

Fizikai forma

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

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 2

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

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


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Dokumentumtár megtekintése

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)
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
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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