Abstract
This chapter describes the purification procedure of uridine phosphorylase enzyme from rat liver. Uridine phosphorylase occupies an important amphibolic position in metabolism because of its role in the degradation of pyrimidine nucleosides as well as in the salvage pathway for nucleic acid synthesis. Separation of this enzyme from thymidine phosphorylase was achieved first for Escherichia coli and later for mammalian tissues. The enzyme resides mainly in the cytosol fraction of rat liver. Other assay methods of arsenolysis and detection of uracil or ribose formation suffer from the disadvantages that activity is nonlinear with time, and the precision of assay is low. Nuclei and unbroken cells are sedimented at 900 g for 20 min in a Sorvall RC-2B centrifuge. The cytoplasmic fraction is removed; the sediment is rehomogenized with two times its weight of sucrose solution and recentrifuged. Thymidine phosphorylase, on the other hand, has an additional transferase activity that is designated as direct.
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