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Merck

P1506

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type II, ammonium sulfate suspension, 350-600 units/mg protein

Sinónimos:

ATP:pyruvate 2-O-phosphotransferase, PK

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1000 UNITS
42,80 €
5000 UNITS
130,00 €
25000 UNITS
507,00 €
50000 UNITS
755,00 €

42,80 €


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1000 UNITS
42,80 €
5000 UNITS
130,00 €
25000 UNITS
507,00 €
50000 UNITS
755,00 €

About This Item

Número de CAS:
Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

42,80 €


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origen biológico

rabbit muscle

tpo

Type II

Formulario

ammonium sulfate suspension

actividad específica

350-600 units/mg protein

mol peso

237 kDa

condiciones de almacenamiento

(Tightly closed)

técnicas

ligand binding assay: suitable

color

white

actividad extraña

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

temp. de almacenamiento

2-8°C

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Descripción general

Research Area: Cell Signaling

Pyruvate kinase from rabbit muscle catalyzes ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate.[1]Pyruvate kinase, an enzyme,[2] is found in a tetrameric or a dimeric form.[3] PKM1, PKM2, PKR, and PKL are the four mammalian pyruvate kinase isoforms.[2]

Aplicación

Pyruvate kinase from rabbit muscle has been used in:

  • a structural study to understand the reaction mechanism of the final step in glycolysis. [4]
  • a study to investigate ATP-dependent phosphorylation of α-substituted carboxylic acids. [1]
  • enzyme assays.[5]

Acciones bioquímicas o fisiológicas

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 from rabbit muscle can be activated by histidine and inhibited by low levels of zinc (Zn2+). [6] In the glycolytic pathway, pyruvate kinase (PK) functions as a terminal enzyme, catalyzing the conversion of phosphoenolpyruvate to pyruvate and the synthesis of ATP through substrate-level phosphorylation. Tetrameric structures of PK are more active and have a high affinity for phosphoenolpyruvate (PEP), whereas dimeric structures are less active and have a low affinity for PEP.[3] PK from rabbit muscle possesses positive kinetic cooperativity (Hill coefficient> 1.35) of the phosphoenol pyruvate and adenosine diphosphate(ADP) binding sites.[7]

Definición de unidad

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

Forma física

Suspension in 3.2 M (NH4)2SO4 solution, pH 6

Nota de análisis

Protein determined by biuret.

sustrato

Referencia del producto
Descripción
Precios

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Listados normativos

Los listados normativos se proporcionan para los productos químicos principalmente. Para los productos no químicos sólo se puede proporcionar información limitada. Si no hay ninguna entrada, significa que ninguno de los componentes está en la lista. Es obligación del usuario garantizar el uso seguro y legal del producto.

EU REACH Annex XVII (Restriction List)

CAS No.

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Certificados de análisis (COA)

Lot/Batch Number

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Visite la Librería de documentos

S Strumilo et al.
Zhurnal evoliutsionnoi biokhimii i fiziologii, 51(2), 103-107 (2015-06-02)
Some catalytic and kinetic properties of pyruvate kinase (PK, EC 2.7.1.40) isolated from the heart and skeletal muscles of rabbits and hares with a 9-16-fold purification were studied. The initial specific activity of the enzyme in hare heart homogenates was
Inhibitory effect of Zn2+ on rabbit muscle pyruvate kinase and reactivation by histidine.
Tamaki N.
J. Nutr. Sci. Vitaminol., 27, 107-116 (1981)
Xun Chen et al.
Cancer cell international, 20(1), 523-523 (2020-12-10)
Pyruvate kinase is a terminal enzyme in the glycolytic pathway, where it catalyzes the conversion of phosphoenolpyruvate to pyruvate and production of ATP via substrate level phosphorylation. PKM2 is one of four isoforms of pyruvate kinase and is widely expressed
D E Ash et al.
Archives of biochemistry and biophysics, 228(1), 31-40 (1984-01-01)
Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate (F. J. Kayne (1974) Biochem. Biophys. Res. Commun. 59, 8-13). An investigation of anologous reactions with other alpha-substituted carboxylic acids reveals several new substrates for such
Glucokinase in Atlantic Halibut (Hippoglossus hippoglossus) Brockmann Bodies
Tranulis MA, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 116, 367-370 (1997)

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Preguntas

1–2 de 2 Preguntas  
  1. この製品(P1506, ピルビン酸キナーゼ)についてご質問があります。 この製品の比活性は350-600 units/mg proteinと記載ありますが、濃度としてU/mLはお分かりになるのでしょうか。 Lot毎に異なることかもしれませんので、試薬の瓶そのものに記載があったりするのでしょうか(データシートには記載が見当たらない)。 ご確認のほど、よろしくお願いいたします。

    1 respuesta
    1. The concentration in U/mL can be determined using the Enzymatic Activity and the mg protein/mL value reported on the lot specific Certificate of Analysis. For example, a lot has a reported Enzymatic Activity of 359 units/ mg protein and 13.7 mg protein/ mL will have a concentration 4918.3 units/ml. Please see the link below to review a sample or lot specific Certificate:
      https://www.sigmaaldrich.com/US/en/product/sigma/p1506#product-documentation

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  2. Hi, How long can this be stored in the fridge?

    1 respuesta
    1. This product is not assigned an expiration date or retest date. Products that are robust in nature and extremely stable, in the original unopened container, are not assigned an expiration date or retest schedule. These products will have no dating reported on either the label or the Certificate of Analysis. Products that are not assigned an expiration or retest date are covered by a warranty period of 1 year from the date of product shipment.

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