Ｌ‐リジンのＪ１ファージに対する不活化作用

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タイトル別名
  • Inactivating-Effect of L-Lysine on Phage J1
  • L リジン ノ J1 ファージ ニ タイスル フカツカ サヨウ

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The inactivating-effect of L-lysine (Lys) on phage was investigated, using phage J1 of Lactobacillus casei asw a model.<br> The inactivation of phage by Lys was irreversible. The rate of inactivation was dependent on the concentration of Lys, being maximum at 0.3M. It was also dependent on pH, being maximum at pH 8, and on temperature, being nil at 0_??_4°C, but progressively more rapid from 20°C to 46°C. The addition of metal cations (Na+, K+, Mg2+, Mn2+, Ca2+ etc.), acidic amino acids, or nucleotides into the reaction mixture inhibited the inactivation of phage by Lys. In contrast, basic amino acids enhanced it. Chelating agents, neutral amino acids, bases, or nucleosides little affected the inactivation. The interaction of Lys with DNA extracted from the phage was observed, but the protein moiety of phage had little interaction with Lys. Nα-acetyl-Lys, Nα -benzyloxycarbonyl (Z)-Lys, Nα, _??_, -diZ-Lys and Lys ethyl ester exhibited no inactivating-effect, whereas N_??_-Z-Lys methyl ester and n-hexylamine exhibited the same effect as Lys.<br> The above results suggest that the interaction of the ε-amino group of Lys with the phosphate residues of phage DNA is primarily responsible for the inactivation of phage.<br> Sucrose and CsCl density gradient centrifugation analyses and electron microscopic observations of the Lys-inactivated phage revealed the release of phage DNA from its protein covering.

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