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Merck

PK-RO

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Sinónimos:

PK

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UNSPSC Code:
12352204
Número CE:
NACRES:
NA.54
Specific activity:
~200 units/mg protein (at 25 °C (500 U/mg at 37 °C) with PEP as the substrate.)
Biological source:
rabbit muscle

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biological source

rabbit muscle

form

suspension

specific activity

~200 units/mg protein (at 25 °C (500 U/mg at 37 °C) with PEP as the substrate.)

packaging

pkg of 1 mL (10128155001 [10 mg]), pkg of 10 mL (10128163001 [100 mg])

manufacturer/tradename

Roche

optimum pH

7.0-7.5

storage temp.

2-8°C

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Este artículo
P150610109045001P9136
specific activity

~200 units/mg protein (at 25 °C (500 U/mg at 37 °C) with PEP as the substrate.)

specific activity

350-600 units/mg protein

specific activity

~200 units/mg protein (At 25 °C with PEP as the substrate.)

specific activity

350-600 units/mg protein

biological source

rabbit muscle

biological source

rabbit muscle

biological source

rabbit muscle

biological source

rabbit muscle

form

suspension

form

ammonium sulfate suspension

form

solution

form

lyophilized powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C (−15°C to −25°C)

storage temp.

−20°C

optimum pH

7.0-7.5

optimum pH

-

optimum pH

7.0-7.5

optimum pH

-

Quality Level

100

Quality Level

200

Quality Level

100

Quality Level

200

General description

ATP:pyruvate 2-O-phosphotransferase
Pyruvate kinase has a molar mass of 237,000 and exists as a tetramer. Each polypeptide chain of this tetramer has a molar mass of 57,200. The enzyme contains two identical catalytic particles called protomers. Each of these protomers contains two polypeptide chains. Each protomer contains one site each for Mn2+ and phosphoenolpyruvate.[1]

Application

Pyruvate kinase has been used to measure ATPase activity[2] and in the determination of adenylate concentration.[3]

Biochem/physiol Actions

Pyruvate kinase catalyzes the irreversible conversion of P-enolpyruvate and ADP to pyruvate and ATP with the utilization of a proton. The first step is the transfer of phosphate group from P-enolpyruvate to ADP with the formation of bound enolate of pyruvate and ATP. In the second step, a proton is added to enolate to generate the keto form of pyruvate. Apart from this, the enzyme exhibits other activities, such as ATP- and bicarbonate-dependent ATPase, phosphorylation of fluoride and hydroxylamine, ATP-dependent phosphorylation of glycolate, and decarboxylation of oxaloacetate.[4]

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Preparation Note

Activator: PK requires Mg2+ (or Mn2+, Co2+) and K+ (or NH4+, Rb+) for full activity.

Analysis Note

Contaminants: <0.001% GK, <0.002% “NADH oxidase”, and ATPase, each, <0.01% enolase, LDH, and myokinase, each

Other Notes

For life science research only. Not for use in diagnostic procedures.

Clase de almacenamiento

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

No data available

flash_point_c

No data available


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Monika Ostaszewska et al.
Journal of plant physiology, 171(7), 549-558 (2014-03-25)
Sulphur, as a constituent of amino acids (cysteine and methionine), iron-sulphur clusters, proteins, membrane sulpholipids, glutathione, glucosinolates, coenzymes, and auxin precursors, is essential for plant growth and development. Absence or low sulphur concentration in the soil results in severe growth
Ilana M Nodelman et al.
EMBO reports, 14(12), 1098-1103 (2013-10-16)
Chromatin remodellers are ATP-dependent motor proteins that physically reposition and reorganize nucleosomes. Chd1 and Iswi-type remodellers possess a DNA-binding domain (DBD) needed for efficient nucleosome mobilization; however, it has not been clear how this domain physically contributes to remodelling. Here
Metabolic control and structure of glycolytic enzymes. 3. Dissociation and subunit structure of rabbit muscle pyruvate kinase.
M A Steinmetz et al.
Biochemistry, 5(4), 1399-1405 (1966-04-01)
T M Larsen et al.
Biochemistry, 33(20), 6301-6309 (1994-05-24)
The molecular structure of rabbit muscle pyruvate kinase, crystallized as a complex with Mn2+, K+, and pyruvate, has been solved to 2.9-A resolution. Crystals employed in the investigation belonged to the space group P1 and had unit cell dimensions a

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