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The Activity of Haemophilus Influenzae ß-Lactamase

  • S. Kattan
  • P. Cavanagh
  • J. D. Williams
Part of the Chemotherapy book series (CT, volume 5)

Summary

H. influenzae ß-lactamase was found to closely resemble the E. coli TEM, ß-lactamase in its substrate profile and rate of hydrolysis of benzyl penicillin, ampicillin and cephaloridine. The permeability barrier to ampicillin and benzyl penicillin observed in the E. coli strain was not detected in the Haemophilus influenzae strain as judged by the activity of whole cell suspensions. It is concluded therefore that this difference is responsible for the smaller amounts of ampicillin required to inhibit ß-lactamase producing strains of H.influenzae compared to strains of E. coli producing ß-lactamase.

Keywords

Benzyl Penicillin Haemophilus Influenzae Permeability Barrier Minimum Inhibitory Concentra Substrate Profile 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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  6. Williams, J.D., Kattan, S., Cavanagh, P. Penicillinase production in Haemophilus influenzae. Lancet, ii, 103 (1974).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • S. Kattan
    • 1
  • P. Cavanagh
    • 2
  • J. D. Williams
    • 1
  1. 1.Department of Medical MicrobiologyThe London Hospital Medical CollegeLondonUK
  2. 2.Public Health Laboratory ServiceStoke-on-TrentUK

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