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P9136

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type III, lyophilized powder, 350-600 units/mg protein

Synonyme(s) :

ATP:pyruvate 2-O-phosphotransferase, PK

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About This Item

CAS Number:
9001-59-6
Numéro CE :
2.7.1.40 (BRENDA, IUBMB)
Numéro CE :
232-616-2
Numéro MDL:
MFCD00081946
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

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Source biologique

rabbit muscle

Niveau de qualité

200

Type

Type III

Forme

lyophilized powder

Activité spécifique

350-600 units/mg protein

Poids mol.

237 kDa

Activité étrangère

lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%

Température de stockage

−20°C

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Cet article
P7768P1903SRP0414
Pyruvate Kinase from rabbit muscle Type III, lyophilized powder, 350-600 units/mg protein

P9136

Pyruvate Kinase from rabbit muscle

Pyruvate Kinase from rabbit muscle Type VII, buffered aqueous glycerol solution, 350-600 units/mg protein

P7768

Pyruvate Kinase from rabbit muscle

Pyruvate Kinase from Bacillus stearothermophilus Type VIII, lyophilized powder, 100-300 units/mg protein

P1903

Pyruvate Kinase from Bacillus stearothermophilus

PKLR Var2 active human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

SRP0414

PKLR Var2 active human

specific activity

350-600 units/mg protein

specific activity

350-600 units/mg protein

specific activity

100-300 units/mg protein

specific activity

-

biological source

rabbit muscle

biological source

-

biological source

Bacillus sp. (B. stearothermophilus)

biological source

human

form

lyophilized powder

form

buffered aqueous glycerol solution

form

lyophilized powder

form

aqueous solution

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−70°C

mol wt

237 kDa

mol wt

237 kDa

mol wt

-

mol wt

59 kDa

foreign activity

lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%

foreign activity

lactic dehydrogenase and creatine phosphokinase ≤0.01%, phosphoglucomutase and myokinase ≤0.05%

foreign activity

-

foreign activity

-

Description générale

Pyruvate Kinase (PK) is a glycolysis enzyme[1] and has four isozymes L, R, M1, and M2. The L isozyme is localized in gluconeogenic tissues, particularly in the liver. Whereas the R and M1 are localized in the adult skeletal muscles, heart, brain and erythrocytes, respectively.[2] M2 is localized in the nucleus of the cells.[1]

Application

Pyruvate Kinase from rabbit muscle has been used to convert adenosine diphosphate (ADP) to adenosine triphosphate (ATP) in Pseudomonas putida cells.[3]
Pyruvate kinase has been used in plant spectrophotometric assays to measure ATP hydrolysis [4]. Pyruvate kinase is also used to study pyruvate kinase (PK) deficiency [5].

Actions biochimiques/physiologiques

Molecular Weight: 237 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa.
Isoelectric Point: 7.6
Optimal pH: ∼7.5
Optimal Temperature: 25°C
ΕA280 = 0.54 for 1 mg(p)/ml, 1 cm path
Reported KM values are ATP (0.86 mM), pyruvate (10 mM), ADP (0.3 mM), and PEP (0.07 mM) in Tris buffer at pH 7.4 and 30 °C. Pyruvate kinase is highly specific for phosphoenolpyruvate, but can utilize other dinucleotide triphosphates as substrates in place of ATP including GTP, ITP, dATP, UTP, and CTP.
Pyruvate kinase (PK) catalyzes an important process of transferring phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP). This reaction results in the conversion of PEP to pyruvate and adenosine triphosphate (ATP).[1][6] Pyruvate kinase plays a major role in glycolysis and gluconeogenesis.[1][7] High levels of pyruvate kinase M2 (PKM2) inhibits cell proliferation and tumor growth.[8] Deficiency of PK in red blood cells (RBC) leads to non-spherocytic hemolytic anaemia.[9] In human erythrocytes, deficiency of PK induces a protective effect against Plasmodium falciparum.[6]

Définition de l'unité

One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C.

Remarque sur l'analyse

Protein determined by biuret.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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    Certificats d'analyse (COA)

    Lot/Batch Number
    SLCD4181
    SLBX3105
    SLBT9131
    SLBS8585
    SLBN7642V

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    Applied Energy, 88(12), 5188-5192 (2011)
    I M Prudnikov et al.
    Fiziologicheskii zhurnal, 35(6), 98-100 (1989-11-01)
    The suggested technique allows revealing the transport-specific dye (primulin) and catecholamine fluorescence simultaneously in the same cell of brain. Intense fluorescence is observed when brain tissue is quickly dehydrated and embedded in the epoxy resin. The same method is suggested
    S Trumbeckaitė et al.
    Phytotherapy research : PTR, 27(4), 499-506 (2012-05-26)
    In this study, the direct influence of bilberry (Vaccinium myrtillus) fruit extracts (aqueous and ethanolic) rich in anthocyanins on the oxidative phosphorylation of isolated rat heart mitochondria was investigated in vitro. Higher concentrations of bilberry extracts concentration-dependently inhibited mitochondrial state
    V A Otellin et al.
    Arkhiv anatomii, gistologii i embriologii, 80(1), 26-29 (1981-01-01)
    A possibility to study associative and projective connections of the optic cortical fields by the method of luminescent revealing of primuline retrograde transport has been demonstrated in the experiments with cats. Initial neurons of the connective systems have been revealed
    Rose Scott-Moncrieff and the dawn of (bio)chemical genetics.
    Martin C.
    The Biochemical Journal, 38(2), 48-53 (2016)
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