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Merck

P2014

Sigma-Aldrich

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Sinónimos:

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
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Formulario

lyophilized powder

actividad específica

≥60 units/mg protein

composición

Protein, 20-40% biuret

actividad extraña

ATPase ≤0.5%
phosphorylase a ≤1%
phosphorylase b ≤5%

temp. de almacenamiento

−20°C

Descripción general

Phosphorylase kinase contains four subunits each containing an α, β, γ, and sigma component. The sigma component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit. [1]

Aplicación

Phosphorylase kinase from rabbit muscle has been used in a study to assess features of glycogen phosphorylase. [2] It has also been used in a study to investigate the activation of different forms of muscle phosphorylase kinase by actin. [3]

Definición de unidad

One unit will form 1.0 μmolar unit of phosphorylase a from phosphorylase b per min at pH 7.7 at 30°C in the presence of ATP.

Forma física

Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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S Camus et al.
Oncogene, 31(39), 4333-4342 (2011-12-20)
Angiogenesis is essential for development and tumor progression. With the aim of identifying new compound inhibitors of the angiogenesis process, we used an established enhanced green fluorescent protein-transgenic zebrafish line to develop an automated assay that enables high-throughput screening of
K F Chan et al.
The Journal of biological chemistry, 257(10), 5956-5961 (1982-05-25)
Aspects of the molecular interaction and subunit structure of rabbit skeletal muscle phosphorylase kinase, (alpha beta gamma delta)4, were investigated. Exogenous addition of the delta subunit (calmodulin) stimulated the activities of nonactivated phosphorylase kinase and the alpha gamma delta complex
Simona Fermani et al.
The Journal of biological chemistry, 287(25), 21372-21383 (2012-04-20)
Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized
G Kamp
Biological chemistry Hoppe-Seyler, 367(2), 109-117 (1986-02-01)
The activities of glycogen phosphorylases a and b from the body wall musculature of the marine worm Arenicola marina (Annelida, Polychaeta) were determined after various periods of anoxia. Already under normoxic conditions one third of the total activity was produced
Monica Balsera et al.
Planta, 237(2), 619-635 (2012-12-12)
Uncovered in studies on photosynthesis 35 years ago, redox regulation has been extended to all types of living cells. We understand a great deal about the occurrence, function, and mechanism of action of this mode of regulation, but we know little

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