The activity of thymidine phosphorylase obtained from human uterine leiomyomas and studied in the presence of pyrimidine derivatives.
Partially purified samples of thymidine phosphorylase were obtained from four preparations of human uterine leiomyomas and uteri using the method of Yoshimura et al. (1990), Biochim. Biophys. Acta 1034, 107-113. Among the studied twelve pyrimidine derivatives, 5-bromouracil, 5-nitrouracil, 5-fluorouracil, 6-aminouracil, 4, 6-dihydroxy-5-nitropyrimidine are competitive inhibitors, while allyloxymethylthymine is an uncompetitive inhibitor of thymidine phosphorylase activity, 6-benzyl-2-thiouracil inhibits the activity of the enzyme in a mixed way. The most potent inhibitor of the thymidine phosphorylase activity is 5-bromouracil and uracil the weakest one. Stronger inhibition of these compounds on the activity of thymidine phosphorylase was found in uterine leiomyomas than in uteri.
Miszczak-Zaborska
E
E
Department of Biochemistry, Medical University of Lódź, Poland.
Woźniak
K
K
D000328:Adult; D000964:Antimetabolites, Antineoplastic / Q000494:pharmacology*; D005260:Female; D006801:Humans; D007700:Kinetics; D007889:Leiomyoma / Q000201:enzymology*; D008875:Middle Aged; D011743:Pyrimidines / Q000494:pharmacology; D013939:Thymidine Phosphorylase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D014594:Uterine Neoplasms / Q000201:enzymology*; D014599:Uterus / Q000201:enzymology*
D000964:Antimetabolites, Antineoplastic; D011743:Pyrimidines; D013939:Thymidine Phosphorylase