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Merck

P6635

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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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-737-0
MDL number:
Numéro CE :
Specific activity:
≥20 units/mg protein
Biological source:
rabbit muscle
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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.)

UniProt accession no.

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

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.

Physical form

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

Other Notes

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.)


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Classe de stockage

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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Contenu apparenté


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
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
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)