Skip to Content
MilliporeSigma
All Photos(1)

Documents

P1261

Sigma-Aldrich

Phosphorylase a from rabbit muscle

lyophilized powder, 20-30 units/mg protein

Synonym(s):

1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

rabbit muscle

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

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
Glycogen Phosphorylase Structures and Function
Fletterick, R. and S. Sprang
Accounts of Chemical Research, 15, 361-369 (1982)
Ian J Tetlow et al.
The Plant cell, 16(3), 694-708 (2004-02-20)
Protein phosphorylation in amyloplasts and chloroplasts of Triticum aestivum (wheat) was investigated after the incubation of intact plastids with gamma-(32)P-ATP. Among the soluble phosphoproteins detected in plastids, three forms of starch branching enzyme (SBE) were phosphorylated in amyloplasts (SBEI, SBEIIa
R C Mead et al.
Biochimica et biophysica acta, 701(2), 173-179 (1982-02-18)
Polychlorinated biphenyls, polychlorinated biphenylols and polybrominated biphenyls inhibited both rabbit muscle phosphorylase a and phosphorylase b (1,4-alpha-D-glucan:orthophosphate alpha-d-glucosyltransferase, EC 2.4.1.1). The degree of inhibition was dependent upon the relative hydrophobicity of the compounds and steric hinderance. 2,4,5,2',4',5'-Hexabromobiphenyl and Firemaster BP-6

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service