Abstract
The glycogen phosphorylase (EC 2.4.1.1) from the mycelium of Phymatotrichum omnivorum was purified by ammonium sulfate fractionation, gel nitration 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 K m 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(β-aminoethyl ether)- N,N′-tetraacetic acid, and Cu 2+ were the potent inhibitors of the glycogen phosphorylase activity, Ca 2+, Cu 2+, Co 2+, and Fe 2+ stimulated the enzyme activity. The enzyme preparation was stable at 4 °C during a period of 30 days.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
