By Albert Neuberger, L. L. M. Van Deenen, Giorgio Semenza

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Skipper and his colleagues [119] had shown that injection of these compounds into tumor-bearing mice (sarcoma 180) resulted in the inhibition of the tumor growth and an inhibition of incorporation of purine precursors into nucleic acids. The compounds therefore had a potential for use in cancer chemotherapy. When Bruce Levenberg [69,120,121] applied these drugs to our enzymatic system, he found that inosinic acid synthesis from glycine was substantially inhibited and that the rate of inactivation was a function of the concentration of glutamine in the reaction mixture.

This system thus seemed ideal for a study of the types of proteins synthesized during the FST-reaction and their function in subsequent phage development. It was apparent that the proteins coded for by the FST-DNA were the so-called Class I proteins [228]. Three such radioactive proteins were formed from radioactive leucine and identified by polyacrylamide gel electrophoresis. The role of FST-DNA in preparing the host cells for the synthesis of several enzymes (or class II functions) was then demonstrated.

Flaks and Cohen [158,159] had already initiated a program in the synthesis of 5-hydroxymethyl deoxycytidylic acid from methylene tetrahydrofolate and deoxycytidylic acid and were well on their way of the study of the first phageinduced enzyme to be reported, namely dCMP hydroxymethylase. We did not wish to overlap their work, yet needed an entree to the A BACKWARD GLANCE 37 general problem. This clue was provided by an abstract of the Federation Meetings in which Kornberg, Lehman and Simms [160] reported that, although partially purified DNA polymerase from extracts of E.

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