P6635
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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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-737-0
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
rabbit muscle
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
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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.
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.)
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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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
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
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
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
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)
Related Content
Global Trade Item Number
| SKU | GTIN |
|---|---|
| P6635-5MG | 04061834393764 |
| P6635-100MG | 04061834393740 |
| P6635-10MG | 04061832925134 |
| P6635-25MG | 04061834393757 |
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