Partial Purification of a Thymidine Phosphorylase from Human Gastric Cancer

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 t...

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Published inChemical & pharmaceutical bulletin Vol. 34; no. 3; pp. 1219 - 1222
Main Authors SUGATA, SETSURO, KONO, AKIRA, HARA, YASUHIRO, KARUBE, YOSHIHARU, MATSUSHIMA, YOSHIKAZU
Format Journal Article
LanguageEnglish
Published Tokyo The Pharmaceutical Society of Japan 1986
Maruzen
Japan Science and Technology Agency
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Summary: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 1-(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-fluorouracil, an activated form of the antitumor agents, in humn tumor tissues by a TP activity. The values of Km of the TP preparation were 1.68×10-4, 1.72×10-3, 1.33×10-2, and 4.76×10-2M for dThd, 5'-DFUR, Tegafur, and uridine, respectively.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0009-2363
1347-5223
DOI:10.1248/cpb.34.1219