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Sigma-Aldrich

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Synonyme(s) :

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

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About This Item

Numéro CAS:
9001-88-1
Numéro de classification (Commission des enzymes):
2.7.1.38 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131906
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Activité spécifique

≥60 units/mg protein

Composition

Protein, 20-40% biuret

Activité étrangère

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

Température de stockage

−20°C

Description générale

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.

Définition de l'unité

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.

Forme physique

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
M Amin-ul Mannan et al.
Journal of molecular biology, 425(12), 2083-2099 (2013-04-02)
The endoplasmic reticulum transmembrane receptor Ire1 senses over-accumulation of unfolded proteins in the endoplasmic reticulum and initiates the unfolded protein response (UPR). The cytoplasmic portion of Ire1 has a protein kinase domain (KD) and a kinase extension nuclease (KEN) domain
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