Ugrás a tartalomra
Merck

10109045001

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Szinonimák:

PK

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Enzyme Commission szám:
UNSPSC kód:
12352204

biológiai forrás

rabbit muscle

Minőségi szint

form

solution

specifikus aktivitás

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

kiszerelés

pkg of 1 mL (10 mg)

gyártó/kereskedő neve

Roche

optimális pH

7.0-7.5

kiszállítva

dry ice

tárolási hőmérséklet

−20°C (−15°C to −25°C)

Related Categories

Általános leírás

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.

Egyediség

Specific activity: Approximately 200 U/mg at +25°C with PEP as the substrate.

Alkalmazás

Pyruvate Kinase (PK) has been used as a sample in ATPase Assays.
Pyruvate Kinase (PK) has been used in the kinase assay.

Biokémiai/fiziológiai hatások

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. The enzyme also exhibits other activities, such as ATP- and bicarbonate-dependent ATPase, phosphorylation of fluoride and hydroxylamine, ATP-dependent phosphorylation of glycolate, and decarboxylation of oxaloacetate.

Minőség

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

Fizikai forma

Solution in 50% glycerol (v/v), pH approximately 6

Elkészítési megjegyzés

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

Egyéb megjegyzések

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

Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

No data available

Lobbanási pont (C)

No data available


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Matthias M Schneider et al.
Nature communications, 12(1), 5999-5999 (2021-10-16)
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo protein folding and preventing amyloid formation. Chaperones of the Hsp70 family can further disaggregate otherwise irreversible aggregate species such as α-synuclein fibrils, which accumulate in Parkinson's
In vivo evidence for ATPase-dependent DNA translocation by the Bacillus subtilis SMC condensin complex
Wang X, et al.
Molecular Cell, 71(5), 841-847 (2018)
Ryo R Watanabe et al.
iScience, 26(5), 106626-106626 (2023-05-17)
F1-ATPase (F1) is an ATP-driven rotary motor protein ubiquitously found in many species as the catalytic portion of FoF1-ATP synthase. Despite the highly conserved amino acid sequence of the catalytic core subunits: α and β, F1 shows diversity in the
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
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)

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