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- W175689916 abstract "The authors report that hydroxyl radical (/sup ./OH) damage to amino acids (AA) affects their incorporation into E. coli proteins. Modification of AA (Try, Trp, Met, Cys, His, Lys, Asn, Gln) by /sup ./OH was achieved by exposure to /sup 60/Co radiation (1-100 krads at 600 rads/min) in N/sub 2/O saturated water. Following exposure to /sup ./OH, the modified AA were added to suspensions of 8 AA requiring E. coli mutants in M9 medium + glucose. Mutants incubated with the /sup ./OH modified AA underwent less growth than those incubated with unmodified AA; with a declining exponential relationship between /sup ./OH exposure of AA and cell growth. The sensitivity of each AA to modification by /sup ./OH was as follows: Tyr > Trp > Met > Cys > His > Lys > Asn > Gln. Essentially the same pattern was observed for inhibition of mutant growth, which was proportional to the concentration of remaining unmodified (i.e. native) AA. Furthermore, cell growth was restored to normal levels by replenishment of native AA. When AA were irradiated at 50..mu..M and then diluted to concentrations expected to support exponential growth (different for each AA) the radiation doses at which mutant growth was inhibitedmore » by 63% were as follows (in krad): Tyr 41, Trp 48, Met 53, Cys 56, His 57, Lys 68, Asn 80, Gln 116. /sup ./OH-modified /sup 3/H-Trp was not a substrate for protein synthesis in Trp requiring mutants but was taken up by the cells. Modified Trp was also not incorporated in cell-free synthesis experiments. No toxicity was observed when wild type E. coli, in M9 medium + glucose, were supplemented with any of the/sup ./OH-modified AA. Thus /sup ./OH-modified AA do not support E. coli growth.« less" @default.
- W175689916 created "2016-06-24" @default.
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- W175689916 date "1986-05-01" @default.
- W175689916 modified "2023-09-26" @default.
- W175689916 title "Hydroxyl radical modify amino acids and prevent E. coli growth" @default.
- W175689916 hasPublicationYear "1986" @default.
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