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P2014

Sigma-Aldrich

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Synonym(s):

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

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About This Item

CAS Number:
Enzyme Commission number:
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. [1]

Application

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]

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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Laura A Lane et al.
Molecular & cellular proteomics : MCP, 11(12), 1768-1776 (2012-09-12)
Phosphorylase kinase (PhK), a 1.3 MDa enzyme complex that regulates glycogenolysis, is composed of four copies each of four distinct subunits (α, β, γ, and δ). The catalytic protein kinase subunit within this complex is γ, and its activity is
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
Thomas P Howard et al.
Plant signaling & behavior, 6(12), 2026-2030 (2011-11-25)
The chloroplast protein CP12 forms a multi-enzyme complex with the Calvin-Benson cycle enzymes phosphoribulokinase (PRK) and NADP-glyceraldehyde-3-phosphate dehydrogenase (GAPDH). PRK and GAPDH are inactivated when present in this complex, a process shown in vitro to be dependent upon oxidized CP12.
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
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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