P6635
Phosphorylase b from rabbit muscle
lyophilized powder, ≥20 units/mg protein, 2× crystallization
Sinónimos:
α-Glucan Phosphorylase, 1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase, Glycogen Phosphorylase
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-737-0
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
rabbit muscle
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Permítanos ayudarlebiological 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.)
Clase de almacenamiento
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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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)
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)
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
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