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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:
9012-69-5
Numéro de classification (Commission des enzymes):
2.4.1.1 (BRENDA, IUBMB)
Numéro CE :
232-737-0
Numéro MDL:
MFCD00131905
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.77

Source biologique

rabbit muscle

Niveau de qualité

300

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.)

Numéro d'accès UniProt

A0A5F9CLZ9
A0A5F9CRR0
A0A5F9D1C4
A0A5F9DLL9

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)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Marta Migocka-Patrzałek et al.
Cells, 10(4) (2021-05-01)
Glycogen phosphorylase (PG) is a key enzyme taking part in the first step of glycogenolysis. Muscle glycogen phosphorylase (PYGM) differs from other PG isoforms in expression pattern and biochemical properties. The main role of PYGM is providing sufficient energy for
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)
B L Nyomba et al.
The Journal of clinical investigation, 88(5), 1540-1545 (1991-11-01)
Glycogen synthase is activated by protein phosphatase type-1 (PP-1). The spontaneous PP-1 activity accounts for only a small fraction of total PP-1 activity, which can be exposed by trypsin digestion of inhibitor proteins in the presence of Mn2+. We determined
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