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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:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥60 units/mg protein

composition

Protein, 20-40% biuret

foreign activity

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

storage temp.

−20°C

General description

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.

Application

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

Unit Definition

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.

Physical form

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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
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
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
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
Kathryn A Skelding et al.
Advances in experimental medicine and biology, 740, 703-730 (2012-03-29)
Calcium/calmodulin-stimulated protein kinases can be classified as one of two types - restricted or multifunctional. This family of kinases contains several structural similarities: all possess a calmodulin binding motif and an autoinhibitory region. In addition, all of the calcium/calmodulin-stimulated protein

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