1887

Abstract

SUMMARY: The effects of various factors on the release of penicillinase from apparently undamaged cells of a growing culture of were investigated. The enzyme was not eluted from the cells by treating them with high concentrations of salt. Its liberation did not take place at all at 0°, and was nearly completely inhibited at pH values below 6.0, whereas chloramphenicol, at concentrations sufficient to cause complete cessation of growth, caused only partial inhibition of enzyme release. The penicillinase-releasing action of extracts containing heat-labile ‘autolytic’ factors from older cells of the same organism could not be dissociated from their damaging effect on the cell, as indicated by concomitant release of the normally intracellular α-glucosidase. It is concluded that normal penicillinase liberation is controlled by enzymic reactions, as yet unidentified, involving detachment of the enzyme from structures superficially located in the cell envelope.

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/content/journal/micro/10.1099/00221287-26-2-267
1961-10-01
2024-05-05
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References

  1. Fruton J. S. 1960 In The Enzymes, 2nd ed. 4 Chap. 11: Cathepsins. (P. D. Boyer, H. LardyK. Myrback, eds.) New York: Academic Press;
    [Google Scholar]
  2. Glauert A. M., Brieger E. M., Allen J. M. 1961; The fine structure of vegetative cells of Bacillus subtilis. Exp. Cell Res 22:73
    [Google Scholar]
  3. Kushner D. J., Pollock M. R. 1961; The location of cell-bound penicillinase in Bacillus subtilis. J. gen. Microbiol 26:255
    [Google Scholar]
  4. McQuillen K. 1960 In The Bacteria 1 Chap. 6: Bacterial protoplasts. (I. C. GunsalusR. Y. Stanier, eds.) New York: Academic Press Inc;
    [Google Scholar]
  5. Mitchell P. 1961; Experimental approaches to the analysis of specific membrane transport.. IUB/IUBS Symposium on Biological Structure and Function, Stockholm, 1960. (In the Press.)
  6. Mitchell P., Moyle J. 1959; Permeability of the envelopes of Staphylococcus aureus to some salts, amino acids and non-electrolytes.. J. gen. Microbiol. 20:434
    [Google Scholar]
  7. Nomura M., Hosoda J. 1956; Nature of the primary action of the autolysin of Bacillus subtilis. J. Bact. 72:573
    [Google Scholar]
  8. Nomura M., Hosoda J., Yoshikawa H. 1958; Studies on amylase formation by Bacillus subtilis. The mechanism of amylase excretion and cellular structure of Bacillus subtilis J. Biochem. (Tokyo), 45:737
    [Google Scholar]
  9. Pollock M. R. 1961a In The Bacteria 4 Chap. 12: Exoenzymes (I.C. GunsalusR. Y. Stanier, eds.) New York: Academic Press;
    [Google Scholar]
  10. Pollock M. R. 1961b; The measurement of the liberation of penicillinase from Bacillus subtilis. J. gen. Microbiol. 26:239
    [Google Scholar]
  11. Pollock M. R., Kramer M. 1958; Intermediates in the bio-synthesis of bacterial penicillinase.. Biochem. J. 70:665
    [Google Scholar]
  12. Richmond M. H. 1959a; Formation of a lytic enzyme by a strain of Bacillus subtilis. Biochim. biophys. Acta, 33:78
    [Google Scholar]
  13. Richmond M. H. 1959b; Properties of a lytic enzyme produced by a strain of Bacillus subtilis. Biochim. biophys. Acta, 33:92
    [Google Scholar]
  14. Salton M. R. J. 1960 In The Bacteria 1 Chap. 3: Surface layers of the bacterial cell. (I. C. GunsalusR. Y. Stanier, eds.) New York: Academic Press Inc;
    [Google Scholar]
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