P1261
Phosphorylase a from rabbit muscle
lyophilized powder, 20-30 units/mg protein
Synonym(s):
1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase
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About This Item
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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
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)
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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
Glycogen Phosphorylase Structures and Function
Fletterick, R. and S. Sprang
Accounts of Chemical Research, 15, 361-369 (1982)
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
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
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)
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