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Merck

PK-RO

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Sinónimos:

PK

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352204

biological source

rabbit muscle

Quality Level

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

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.

Application

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

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.

Quality

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

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.

Other Notes

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

No data available

flash_point_c

No data available


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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
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
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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