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P2014

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Synonym(e):

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

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Über diesen Artikel

CAS-Nummer:
EG-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥60 units/mg protein

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Unterstützung erhalten

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]

Physical form

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

Other Notes

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.

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Die Dokumentenbibliothek aufrufen

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
Eijiro Ozawa
Proceedings of the Japan Academy. Series B, Physical and biological sciences, 87(8), 486-508 (2011-10-12)
It had long been one of the crucial questions in muscle physiology how glycogenolysis is regulated in connection with muscle contraction, when we found the answer to this question in the last half of the 1960s. By that time, the
G V Silonova et al.
Biokhimiia (Moscow, Russia), 49(1), 127-135 (1984-01-01)
The activation of different forms of muscle phosphorylase kinase by actin has been studied. F-actin which is polymerized by 2 mM MgCl2 is a more effective activator of phosphorylase kinase than F-actin polymerized by 50 mM KCl. There is evidence
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

Global Trade Item Number

SKUGTIN
P2014-2.5KU04061832925103
P2014-1KU04061832925097

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