Substrate Specificity of a Thymidine Phosphorylase in Human Liver Tumor

Akira Kono, Yasuhiro Hara, Setsuro Sugata, Yoshikazu Matsushima, Tohru Ueda

研究成果: Article査読

28 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1919-1921
ページ数3
ジャーナルChemical and Pharmaceutical Bulletin
32
5
DOI
出版ステータスPublished - 1984

ASJC Scopus subject areas

  • 化学一般
  • 創薬

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