Skip to Content
Merck
All Photos(2)

Key Documents

View All Documentation

P6635

Sigma-Aldrich

Phosphorylase b from rabbit muscle

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

Synonym(s):

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

Sign Into View Organizational & Contract Pricing
All Photos(2)

About This Item

CAS Number:
9012-69-5
Enzyme Commission number:
2.4.1.1 (BRENDA, IUBMB)
EC Number:
232-737-0
MDL number:
MFCD00131905
UNSPSC Code:
12352204
NACRES:
NA.77

biological source

rabbit muscle

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

97,200 Da by calculation

purified by

2× crystallization

storage condition

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

technique(s)

mass spectrometry (MS): suitable

impurities

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

UniProt accession no.

A0A5F9CLZ9
A0A5F9CRR0
A0A5F9D1C4
A0A5F9DLL9

foreign activity

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

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

General description

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

Biochem/physiol Actions

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.

Packaging

Package size based on protein content.

Unit Definition

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.)

Physical form

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000427562
0000427562
0000409492
0000377106
0000374875

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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)
Cécile Mathieu et al.
The FEBS journal, 284(4), 546-554 (2016-10-27)
Glycogen phosphorylase (GP) is the key enzyme that regulates glycogen mobilization in cells. GP is a complex allosteric enzyme that comprises a family of three isozymes: muscle GP (mGP), liver GP (lGP), and brain GP (bGP). Although the three isozymes
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
J Tandecarz et al.
Molecular and cellular biochemistry, 16(2), 141-148 (1977-07-05)
Rabbit muscle phosphorylase b was found to be capable of forming protein bound alpha-1,4 glucosyl chains upon incubation of the enzyme with appropriate concentrations of glucose-1-phosphate with no primer addition (unprimed synthesis). This activity would only be present in a
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service