type	Journal Article
authors	Sambandam, T.; Gunasekaran, M.
title	Purification and properties of phosphorylase from Phymatotrichum omnivorum
journal	Arch Biochem Biophys
Activity	2.4.1.1
ui	87212045
year	(1987)
volume	254
number	2
pages	579-85.
keywords	Cations, Divalent
abstract	The glycogen phosphorylase (EC 2.4.1.1) from the mycelium of Phymatotrichum omnivorum was purified by ammonium sulfate fractionation, gel filtration on Sephacryl S-200, and DEAE-cellulose ion-exchange chromatography to more than 100-fold. The purified enzyme was homogeneous; this was confirmed by polyacrylamide gel electrophoresis. Sodium dodecyl sulfate-gel electrophoresis indicated the relative molecular size of the enzyme was around 145,000. The approximate molecular weight by gel filtration was 116,000. The optimum pH of the enzyme was 7.0 and the enzyme was more specific for glycogen, with a Km value of 0.36 mg/ml. Nucleotides AMP, ADP, and ATP and compounds containing an "SH" group inhibited the enzyme activity. Diethyldithiocarbamate, EDTA, ethylene glycol bis(beta-aminoethyl ether)-N,N'-tetraacetic acid, and Cu2+ were the potent inhibitors of the glycogen phosphorylase activity, Ca2+, Cu2+, Co2+, and Fe2+ stimulated the enzyme activity. The enzyme preparation was stable at 4 degrees C during a period of 30 days.
last changed	2002/11/12 16:17