Abstract

Thymidine kinase, the enzyme in the pyrimidine salvage pathway, and its isozymes were examined in 10 specimens of normal mammary gland, 10 fibroadenomas and 11 adenocarcinomas in human breasts. The average thymidine kinase activities in fibroadenomas and adenocarcinomas were about 3 and 8 times that in normal mammary gland. The mammary thymidine kinase isozymes were separated into two types by diethylaminoethyl (DEAE) cellulose column chromatography. The activity of the thymidine kinase isozyme eluted with 0.1 M sodium chloride in buffer was twofold higher in fibroadenomas and fourfold higher in adenocarcinomas than that in normal tissue. In adenocarcinomas, but not fibroadenomas, the activity of the other isozyme eluted with buffer alone was increased to 22-fold that in normal tissues. As the activity of the latter isozyme was not affected by deoxycytidine triphosphate, it may be involved closely in DNA replication.

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