Partial Purification of a Thymidine Phosphorylase from Human Gastric Cancer

Setsuro Sugata, Yoshiharu Karube, Akira Kono, Yoshikazu Matsushima, Yasuhiro Hara

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13 Citations (Scopus)


A thymidine phosphorylase (TP) preparation was partially purified from human gastric cancer (poorly differentiated adenocarcinoma). The specific activity of the final preparation represented a 379-fold purification of the 7000g supernatant of tissue homogenate. The phosphorolytic activities toward thymidine (dThd), 5’-deoxy-5-fluorouridine (5’-DFUR), and l-(tetrahydro-2-furanyl)-5-fluorouracil (Tegafur) remained closely in parallel during the whole purification procedure. The results provide evidence in support of the assumption that 5’-DFUR and Tegafur are converted into 5-fiuorouracil, an activated form of the antitumor agents, in human tumor tissues by a TP activity. The values of Kmof the TP preparation were 1.68 x 10~4, 1.72 x 10–3, 1.33 x 10–2, and 4.76 x 10-2 m for dThd, 5’-DFUR, Tegafur, and uridine, respectively.

Original languageEnglish
Pages (from-to)1219-1222
Number of pages4
JournalChemical and Pharmaceutical Bulletin
Issue number3
Publication statusPublished - 1986 Jan 1


  • 5-fluorouracil
  • 5’-deoxy-5-fluorouridine
  • gastric cancer
  • human tumor
  • l-(tetrahydro-2-furanyl)-5-fluorouracil
  • thymidine
  • thymidine phosphorylase
  • uridine
  • uridine phosphorylase

ASJC Scopus subject areas

  • General Chemistry
  • Drug Discovery


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