Elemental and Amino Acid Composition of Purified Plague Toxin

Bent, Donald F.; Rosen, Harvey M.; Levenson, Stanley Μ.; Lindberg, Robert B.; Ajl, Samuel J.

doi:10.3181/00379727-95-23159

Cited by 6 publications

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“…Concomitantly, proteins are made under inhibited conditions which require little or no unaltered tryptophan for their formation. According to the amino acid analysis of murine toxin by Bent et al (1957), its tryptophan 11.1 17.8 indole * Analogue concentrations were 20 ,Ag/ml for experiment 1, and 50 ,jg/ml of 4-MT and 20 jug/ml of indole for experiment 2. content is approximately 3.5% by weight. Our analyses (Table 5) show that the tryptophan content of cells grown on synthetic medium is a little over 2%.…”

Section: Discussionmentioning

confidence: 99%

SELECTIVE INHIBITION BY TRYPTOPHAN ANALOGUES OF MURINE TOXIN SYNTHESIS IN PASTEURELLA PESTIS

Montie

Ajl

1964

J Bacteriol

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Washed-cell suspensions of Pasteurella pestis, avirulent strain "Tjiwidej," exhibited a preferential inhibition of toxin synthesis relative to total protein formation, when grown in the presence of various tryptophan analogues. Growth was partially inhibited in the presence of methyl analogues. High concentrations of 5-fluorotryptophan induced slight growth-inhibitory effects. However, toxin production was more sensitive to these levels of the analogue. Growth inhibition appeared not to relate to toxin inhibition. Inhibition of toxin synthesis by analogues was reversed by L-tryptophan and indole. Shikimic acid but not anthranilic acid antagonized the action of 4-methyltryptophan on selective toxin synthesis. The formation of tryptophanless protein accounted for continued protein synthesis in tryptophan-depleted cells. Protein resolved by acrylamide gel electrophoresis from crude cell extracts exhibited two toxic protein bands. The synthesis of one toxin-protein band, the less-mobile of the two, appeared to be associated with the membrane fraction of the cell, and was selectively blocked in cells grown in the presence of tryptophan analogues. Cellular tryptophan levels may determine the quantity and quality of proteins made.

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Section: Discussionmentioning

confidence: 99%