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 in | Chemical & pharmaceutical bulletin Vol. 34; no. 3; pp. 1219 - 1222 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
The Pharmaceutical Society of Japan
1986
Maruzen Japan Science and Technology Agency |
Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0009-2363 1347-5223 |
DOI: | 10.1248/cpb.34.1219 |