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. 1976 Dec;128(3):735–740. doi: 10.1128/jb.128.3.735-740.1976

Protein synthesis and degradation in a leucine auxotroph of Escherichia coli.

J J Aguanno, A R Larrabee
PMCID: PMC232763  PMID: 791928

Abstract

The synthesis and degradation of the soluble and sodium dodecyl sulfate-(SDS)-solubilized protein fractions of Escherichia coli were studied in both growing and nongrowing cultures. When separated according to molecular weight on SDS-polyacrylamide gels, the proteins of both fractions of growing cells undergo no measureable differential synthesis or degradation during logarithmic growth. However, when a leucine auxotroph is suspended in medium containing 5.3 muM leucine (a level that will not sustain growth), the SDS-solubilized protein of such a nongrowing culture shows a rapid synthesis of two protein components (32,000 and 12,000 daltons) found only in the out membrane.

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Selected References

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