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- W2034014578 abstract "The influence of a number of amino acid analogs on the ability of Escherichia coli to form proteins was investigated. The analog of tryptophan, 7-azatryptophan, is incorporated into proteins and permits synthesis of proteins and nucleic acids, but the majority of enzymes, and also bacteriophages T1 and T2, did not appear in active forms. Two enzymes, asparate carbamyl transferase and D-serine deaminase, were formed in about half the maximal amounts in the presence of azatryptophan, but not when the tryptophan supply was limited by various other means. Kinetics of inhibition showed that under the experimental conditions 1 and 1.8 minutes were required to establish and reverse the inhibition of β-galactosidase formation, respectively. Phage formation was much more strongly inhibited by the analog than was bacterial growth, thereby providing a kind of chemotherapy. Inhibition of phage development was observed in both the early and late periods after infection. When added a few minutes after the time of infection, azatryptophan inhibited the formation of phage DNA much more strongly than the development of resistance to ultraviolet light; this suggests that the former is not necessary for the latter phenomenon. Protein made in the presence of azatryptophan and isolated in inactive, centrifugable particles had none of the properties of phage protein, but was associated with DNA of the phage type. The analog acts so as to cause major imperfections in the phage protein rather than by simply being incorporated in place of tryptophan." @default.
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- W2034014578 date "1958-01-01" @default.
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- W2034014578 title "Effects of azatryptophan on bacterial enzymes and bacteriophage" @default.
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- W2034014578 doi "https://doi.org/10.1016/0006-3002(58)90340-8" @default.
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