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P1261

Sigma-Aldrich

Phosphorylase a from rabbit muscle

lyophilized powder, 20-30 units/mg protein

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Synonym(s):
1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

form

lyophilized powder

specific activity

20-30 units/mg protein

purified by

2× crystallization

composition

Protein, 30-60% E1%/280

foreign activity

AMP-phosphatase, ATP-phosphatase, debrancher enzyme and phosphorylase phosphatase ≤0.1%
phosphoglucomutase ≤0.25%
phosphorylase b ≤30%

storage temp.

−20°C

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P9544P2014P6635
Sigma-Aldrich

P1261

Phosphorylase a from rabbit muscle

Phosphorylase b from rabbit muscle lyophilized powder, ≥20 units/mg protein, 2× crystallization

P6635

Phosphorylase b from rabbit muscle

specific activity

20-30 units/mg protein

specific activity

≥200 units/mg protein

specific activity

≥60 units/mg protein

specific activity

≥20 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

foreign activity

AMP-phosphatase, ATP-phosphatase, debrancher enzyme and phosphorylase phosphatase ≤0.1%, phosphorylase b ≤30%, phosphoglucomutase ≤0.25%

foreign activity

-

foreign activity

ATPase ≤0.5%, phosphorylase a ≤1%, phosphorylase b ≤5%

foreign activity

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

purified by

2× crystallization

purified by

-

purified by

-

purified by

2× crystallization

General description

Phosphorylase A is the active form of glycogen phosphorylase which converts glycogen and orthophosphate (Pi) to glucose 1-phoshate (G-1-P).

application

Phosphorylase a from rabbit muscle has been used to mix with glycogen for the preparation of limit dextrin. It has also been used to probe the array in oligosaccharide microarray analysis of phosphorylase activity.
Phosphorylase from rabbit muscle has been used in a study to assess the molecular mechanisms of oleanolic acid. It has also been used in a study to describe the conversion of phosphorylase B to A, through a conversion enzyme in the presence of 32P-ATP.

Biochem/physiol Actions

Dimeric phosphorylase b is converted to the more active tetramer, phosphorylase a, by the action of phosphorylase kinase.
Phosphorylase A can be inhibited by these compounds: Polychlorinated biphenyls, polychlorinated biphenylols and polybrominated biphenyls.
Phosphorylase participates in glycogenolysis. Deficiency of phosphorylase leads to several glycogen storage diseases with hepatomegaly.

Unit Definition

One unit will form 1.0 μmole of α-D-glucose 1-phosphate from glycogen and orthophosphate 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 ~45 Cori units.)

Physical form

Lyophilized powder containing β-glycerophosphate and EDTA

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)


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Activity of porcine muscle glycogen debranching enzyme in relation to pH and temperature
Kyla-Puhju M, et al.
Meat Science, 69(1), 143-149 (2005)
Hypoglycemia in the toddler and child
Pediatric Endocrinology, Diabetes, and Metabolism, 920-955 (2014)
The phosphorylase b to a converting enzyme of rabbit skeletal muscle.
E G KREBS et al.
Biochimica et biophysica acta, 20(1), 150-157 (1956-04-01)
Versatile high-resolution oligosaccharide microarrays for plant glycobiology and cell wall research
Pedersen H L, et al.
The Journal of biological chemistry, M112-M112 (2012)
T C Chang et al.
Plant physiology, 80(2), 534-538 (1986-02-01)
A protein, starch phosphorylase inhibitor, was purified from the root of sweet potato (Ipomoea batatas [L.] Lam. cv Tainon 65). It had a molecular weight of 250,000 and could be composed of five identical subunits. The isoelectric point of the

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