1887

Abstract

SUMMARY:

Ampicillin sensitivity tests and tests for ampicillin inactivation were made with 148 strains of coliform bacilli. A correlation was found in strains of and Klebsiella between ampicillin resistance and inactivation. No correlation was obtained with , whether sensitive or resistant to ampicillin, although small amounts of penicillinase were produced. Ampicillin-sensitive strains of showed even lower amounts of penicillinase. The strains of () were resistant to ampicillin, but also showed low penicillinase levels. No evidence of induction of penicillinase was obtained with or Klebsiella in the presence of methicillin, ampicillin or cephalosporin C. The ampicillin-inactivating enzyme is a β-lactamase, not an amidase. Resistance of ampicillin-sensitive strains of was increased rapidly by serial subcultures but was not associated with higher penicillinase values. Ampicillin was inactivated less rapidly than was benzylpenicillin by penicillinase from an strain.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-30-2-339
1963-02-01
2021-10-18
Loading full text...

Full text loading...

/deliver/fulltext/micro/30/2/mic-30-2-399.html?itemId=/content/journal/micro/10.1099/00221287-30-2-339&mimeType=html&fmt=ahah

References

  1. Abraham E. P., Chain E. 1940; An enzyme from bacteria able to destroy penicillin. Nature, Lond 146:837
    [Google Scholar]
  2. Bondi A., Dietz C. C. 1944; Production of penicillinase by bacteria. Proc. Soc. exp. Biol., N.Y 56:132
    [Google Scholar]
  3. Brumfitt W., Percival A., Carter M. J. 1962; Treatment of urinary tract infections with ampicillin. Lancet i:130
    [Google Scholar]
  4. Czekalowski J. W. 1950; Penicillin inactivators of bacterial origin. J. Path. Bact 62:85
    [Google Scholar]
  5. Geronimus L. H., Cohen S. 1957; Induction of staphylococcal penicillinase. J. Bact 73:28
    [Google Scholar]
  6. Harper G. J. 1943; Inhibition of penicillin in routine culture media. Lancet ii:569
    [Google Scholar]
  7. Perret C. J. 1954; Iodometric assay of penicillinase. Nature, Lond 174:1012
    [Google Scholar]
  8. Pollock M. R. 1950; Penicillinase adaptation in B. cereus: Adapative enzyme formation in the absence of free filtrate. Brit. J. exp. Path 31:739
    [Google Scholar]
  9. Rolinson G. N., Batchelor F. R., Butterworth D., Cameron-Wood J., Cole M., Eustace G. C, Hart M. V., Richards M., Chain E. B. 1960; Formation of 6-aminopenicillanic acid from penicillin by enzyme hydrolysis. Nature, Lond 187:236
    [Google Scholar]
  10. Rolinson G. N., Stevens S. 1961; Microbiological studies on a broad-spectrum penicillin, ‘Penbritin’. Brit. med. J ii:191
    [Google Scholar]
  11. Stewart G. T., Coles H. M. T, Nixon H. H., Holt R. J. 1961; ‘Penbritin’: an oral penicillin with broad-spectrum activity. Brit. med. J ii:200
    [Google Scholar]
  12. Trafford J. A. P, Maclaren D. M., Lillicrap D. A., Barnes R. D. S, Houston J. C., Knox R. 1962; Ampicillin, a broad-spectrum pencillin. Lancet i987
    [Google Scholar]
  13. Uri J., Sztaricskai F. 1961; Simple, quick methods for detection of 6-aminopenicillanic acid. Nature, Lond 191:1223
    [Google Scholar]
  14. Woodruff H. B., Foster J. W. 1945; Microbiological aspects of pencillin. VII. Bacterial penicillinase. J. Bact 49:7
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-30-2-339
Loading
/content/journal/micro/10.1099/00221287-30-2-339
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error