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- W1441336068 abstract "Publisher Summary This chapter describes the purification procedure of thymidine phosphorylase enzyme from Salmonella typhimurium. In Escherichia coli and Salmonella typhimurium, thymidine phosphorylase plays an important role in the metabolism of thymine auxotrophs and is necessary for the conversion of exogenous thymine to thymidine. In low-thymine-requiring strains, thymidine phosphorylase becomes phenotypically constitutive in strains containing a mutation in deoxyribose-5-phosphate aldolase. Enzyme activity is measured spectrophotometrically by measuring the formation of thymine from thymidine in the presence of sodium arsenate. Purified thymidine phosphorylase can catalyze the conversion of thymidine and deoxyuridine to their respective bases and deoxyribose-l-phosphate. During the latter states of purification, thymidine phosphorylase is quite labile. The use of 2-mercaptoethanol and sucrose during precipitation procedures with ammonium sulfate stabilizes the enzyme. Best results are obtained with a strain of S. typhimurium that is constitutive for thymidine phosphorylase and defective in purine nucleoside phosphorylase." @default.
- W1441336068 created "2016-06-24" @default.
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- W1441336068 date "1978-01-01" @default.
- W1441336068 modified "2023-09-29" @default.
- W1441336068 title "[58] Thymidine phosphoryalse from Salmonella typhimurium" @default.
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- W1441336068 doi "https://doi.org/10.1016/s0076-6879(78)51060-4" @default.
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