Substrate Specificity of a Thymidine Phosphorylase in Human Liver Tumor
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概要
- 論文の詳細を見る
A thymidine phosphorylase preparation was partially purified from human liver tumor tissues (poorly differentiated adenocarcinoma). The substrate specificity of the enzyme was investigated with eleven pyrimidine nucleosides. Thymidine and 2'-deoxyuridine were good substrates, while uridine, 3'-deoxyuridine, 5'-deoxyuridine, and 2', 3'-dideoxy-3'-hydroxy-methyluridine were not. Uridines substituted at the 5-position by a cyano, bromo, or chloro group were also phosphorolyzed by the enzyme, but the activity for 5-fluorouridine was much lower. 5'-Deoxy-5-fluorouridine was also cleaved. Either a 5-substituent or a 2'-deoxy structure seems to be essential for a good substrate.
- 社団法人日本薬学会の論文
- 1984-05-25
著者
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上田 亨
Faculty of Pharmaceutical Science, Hokkaido University
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上田 亨
Faculty Of Pharmaceutical Sciences Hokkaido University
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松島 美一
Kyoritsu College of Pharmacy
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松島 美一
共立薬大
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菅田 節朗
Kyoritsu College of Pharmacy
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河野 彬
Kyushu Cancer Center Research Institute
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原 泰寛
Kyushu Cancer Center Research Institute
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河野 彬
国立九州がんセンター
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上田 亨
北海道大学薬学部
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