Abstract
A procedure is described for the purification of glycogen phosphorylase (α-1,4-glucan:orthophosphate glucosyl transferase, EC 2.4.1.1) from rat and beef kidneys. The Michaelis constants of the components of the phosphorylase-catalyzed reaction and other characteristics of the enzyme are presented. Phosphorylase kinase (ATP: phosphorylase phosphotransferase, EC 2.7.1.38) and phosphatase (phosphorylase phosphohydrolase, EC 3.1.3.17) (free of phosphorylase) also have been partially purified from kidney extracts. Kidney phosphorylase kinase can be substituted for muscle phosphorylase kinase in the phosphorylase activation reaction. From the characteristics of the enzyme, as well as from the results of the activation and inactivation reactions it is concluded that kidney phosphorylase is a form of the enzyme which is different from both liver and muscle phosphorylase.
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.
