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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

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5 MG
$107.00
10 MG
$188.00
25 MG
$310.00
100 MG
$760.96

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5 MG
$107.00
10 MG
$188.00
25 MG
$310.00
100 MG
$760.96

About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77

$107.00


In StockDetails


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biological source

rabbit muscle

Quality Level

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.)

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This Item
P4649P1261P3397
technique(s)

mass spectrometry (MS): suitable

technique(s)

-

technique(s)

-

technique(s)

activity assay: suitable

specific activity

≥20 units/mg protein

specific activity

-

specific activity

20-30 units/mg protein

specific activity

≥100 units/mg protein

form

lyophilized powder

form

powder

form

lyophilized powder

form

ammonium sulfate suspension

storage condition

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

storage condition

-

storage condition

-

storage condition

(Tightly closed)

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

General description

Research area: Cell Signaling

Glycogen phosphorylase (PG), a specialized complex allosteric enzyme[1] has an evolutionarily conserved gene sequence.[2] GP contains a family of three isozymes such as muscle GP (mGP), liver GP (lGP), and brain GP (bGP) in humans.[1]

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[3]
  • in ion mobility-mass spectrometry studies of phosphorylase B ions that have been generated with supercharging reagents, in the charge-reducing buffer[4]
  • for the preparation of p32 labeled phosphorylase A using phosphorylase kinase and [32P]ATP[5]
  • in phosphorylase phosphatase assay[6]
  • in enzyme assay as a positive control to ensure the reaction system for the activity determination was adopted[7]

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[8]. Phosphorylase b is activated by inosine monophosphate[9]. 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.[2] 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.[10]

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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C Villar-Palasi et al.
Proceedings of the National Academy of Sciences of the United States of America, 67(1), 345-350 (1970-09-01)
Phosphorylase b kinase activity, as present in resting muscle in the non-activated form, appears to be ample to account for the fast appearance of phosphorylase a observed with muscle contraction. The kinase activity is repressed by free ATP and stimulated
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)
Shanshan Qin et al.
Frontiers in plant science, 7, 1315-1315 (2016-09-16)
Two isoforms of starch phosphorylase (PHO; EC 2.4.1.1), plastidic PHO1 and cytosolic PHO2, have been found in all plants studied to date. Another starch phosphorylase-like gene, PHO3, which is an ortholog of Chlamydomonas PHOB, has been detected in some plant
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)
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

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