Abstract

Thymidylate synthase (TS; EC 2.1.1.45) catalyzes N5,10-methylenetetrahydrofolate-dependent methylation of dUMP. Purified preparations of the enzyme from regenerating rat liver, L1210 cell and Trichinella spiralis muscle larvae, and recombinant rat hepatoma and mouse L1210 thymidylate synthases, analyzed with the use of SDS Polyacrylamide gel electrophoresis, show heterogeneity, reflected by an additional distinct band (Figure 1; cf. ref. 1), located too close to the main band to enable unequivocal identification resulting from F[3H]dUMP binding. To study this phenomenon, monoclonal antibodies were developed with the use of the recombinant rat hepatoma thymidylate synthase as an antigen.

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