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P6635

Sigma-Aldrich

Phosphorylase b from rabbit muscle

lyophilized powder, ≥20 units/mg protein, 2× crystallization

Synonyme(s) :

α-Glucan Phosphorylase, 1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase, Glycogen Phosphorylase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.77

Source biologique

rabbit muscle

Forme

lyophilized powder

Activité spécifique

≥20 units/mg protein

Poids mol.

97,200 Da by calculation

Produit purifié par

2× crystallization

Conditions de stockage

(Keep container tightly closed in a dry and well-ventilated place)

Technique(s)

mass spectrometry (MS): suitable

Impuretés

~0.01 μmol/mg protein 5′-AMP (This low level will not interfere with phosphorylase and phosphorylase kinase assays.)

Activité étrangère

phosphoglucomutase ≤1.0%
phosphorylase a ≤10%
phosphorylase kinase ≤0.5%
phosphorylase phosphatase, debrancher enzyme, AMPase and ATPase ≤0.1%

Température de stockage

−20°C

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Description générale

Research area: Cell Signaling

Glycogen phosphorylase (PG), a specialized complex allosteric enzyme has an evolutionarily conserved gene sequence. GP contains a family of three isozymes such as muscle GP (mGP), liver GP (lGP), and brain GP (bGP) in humans.

Application

Phosphorylase b from rabbit muscle has been used:
  • in the calibration of Sepharose C1-6B columns while studying the molecular weight of methylamine dehydrogenase subunits
  • in ion mobility-mass spectrometry studies of phosphorylase B ions that have been generated with supercharging reagents, in the charge-reducing buffer
  • for the preparation of p32 labeled phosphorylase A using phosphorylase kinase and [32P]ATP
  • in phosphorylase phosphatase assay
  • in enzyme assay as a positive control to ensure the reaction system for the activity determination was adopted

Actions biochimiques/physiologiques

Phosphorylase b is a non-active form and is present in resting muscles. Phosphorylase b kinase activity increases significantly when the Mg2+:ATP ratio exceeds 1. The breakdown of ATP during muscle contraction is thought to trigger in vivo conversion of phosphorylase b into a. Phosphorylase b is activated by inosine monophosphate. Glycogen phosphorylase (PG) enzyme plays a vital role in the first step of glycogenolysis. In the initial stage of glycogenolysis, glycogen phosphorylase(GP) breaks α-1,4- -glycosidic bonds, releasing the glucose-1-phosphate (G1P)molecule. When incubated with the proper concentrations of glucose-1-phosphate without the addition of primer, rabbit muscle phosphorylase B was found to be capable of forming protein-bound alpha-1,4 glucosyl chains.

Conditionnement

Package size based on protein content.

Définition de l'unité

One unit will form 1.0 μmole of α-D-glucose 1-phosphate from glycogen and orthophosphate in the presence of 5′-AMP, per min at pH 6.8 at 30 °C measured in a system containing phosphoglucomutase, NADP, and glucose 6-phosphate dehydrogenase. (One μmolar unit is equivalent to approx. 45 Cori units.)

Forme physique

Lyophilized powder containing lactose, 5′-AMP, and Mg(OAc)2 (10 μmole per 100 mg protein)

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

F M Vellieux et al.
European journal of biochemistry, 154(2), 383-386 (1986-01-15)
The enzyme methylamine dehydrogenase or primary-amine:(acceptor) oxidoreductase (deaminating) (EC 1.4.99.3) was purified from the bacterium Thiobacillus versutus to homogeneity, as judged by polyacrylamide gel electrophoresis. The native enzyme has a Mr of 123 500 and contains four subunits arranged in
Studies on the allosteric activation of glycogen phosphorylase b by Nucleotides. I. Activation of phosphorylase b by inosine monophosphate.
W J Black et al.
The Journal of biological chemistry, 243(22), 5892-5898 (1968-11-25)
Characterization of the phosphorylase b to a converting activity in skeletal muscle extracts of mice with the phosphorylase b kinase deficiency mutation.
S R Gross et al.
The Journal of biological chemistry, 249(21), 6710-6718 (1974-11-10)
The conversion of lobster muscle phosphorylase a to b and phosphorylase b to a.
R W COWGILL
The Journal of biological chemistry, 234, 3154-3157 (1959-12-01)
Y Kida et al.
The Journal of clinical investigation, 89(2), 610-617 (1992-02-01)
Insulin-stimulated glycogen synthase activity in human muscle is reduced in insulin-resistant subjects. Insulin regulation of human muscle glycogen synthase may require activation of a type-1 protein phosphatase (PP-1). We investigated the change of phosphorylase phosphatase and glycogen synthase activities in

Articles

Glucose metabolism is regulated by the opposing actions of insulin and glucagon. Insulin is released from pancreatic ß cells in response to high blood glucose levels and regulates glucose metabolism through its actions on muscle, liver, and adipose tissue.

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