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P0294

Sigma-Aldrich

Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle

For the Determination of ADP, buffered aqueous glycerol solution

Synonym(s):

PK/LDH enzymes from rabbit muscle

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

form

buffered aqueous glycerol solution

mol wt

59 kDa

concentration

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

storage temp.

−20°C

General description

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.

Application

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

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Thermal activation of `allosteric-like?large-scale motions in a eukaryotic Lactate Dehydrogenase
Katava M, et al.
Scientific Reports, 7, 41092-41092 (2017)
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)
Spontaneous motion in hierarchically assembled active matter
Sanchez T, et al.
Nature, 491(7424), 431-431 (2012)
Keith D Green et al.
Antimicrobial agents and chemotherapy, 55(7), 3207-3213 (2011-05-04)
Aminoglycoside-modifying enzymes (AMEs) constitute the most prevalent mechanism of resistance to aminoglycosides by bacteria. We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased

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