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Modified Substrate Specificity of Cell-bound Penicillinase

Nature volume 198, pages 887–888 (1963)Cite this article

Abstract

PENICILLINASE formed by Bacillus cereus consists of two serologically distinguishable fractions1. One fraction, α-penicillinase, is extracellular and accounts for 90 per cent of the penicillinase activity of a culture. The other fraction, designated as γ-penicillinase, is firmly bound to the cell membrane2. γ-Penicillinase, which is further characterized by susceptibility to iodination1, is definitely not a precursor3, and there is evidence4,5 that it is a derivative of α-penicillinase.

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References

  1. Pollock, M. R., J. Gen. Microbiol., 15, 154 (1956).

    Article  CAS  Google Scholar 

  2. Sheinin, R., J. Gen. Microbiol., 21, 124 (1959).

    Article  CAS  Google Scholar 

  3. Pollock, M. R., and Kramer, M., Biochem. J., 70, 665 (1958).

    Article  CAS  Google Scholar 

  4. Citri, N., Biochim. Biophys. Acta, 27, 277 (1958).

    Article  CAS  Google Scholar 

  5. Citri, N., Bull. Res. Counc. Israel, 9, A, 28 (1960).

    Google Scholar 

  6. Citri, N., Garber, N., and Sela, M., J. Biol. Chem., 235, 3454 (1960).

    PubMed  CAS  Google Scholar 

  7. Pollock, M. R., Brit. J. Exp. Path., 31, 739 (1950).

    PubMed  CAS  Google Scholar 

  8. Rolinson, G. N., Stevens, S., Batchelor, F. R., Cameron-Wood, J., and Chain, E. B., Lancet, ii, 564 (1960).

  9. Garber, N., and Citri, N., Biochim. Biophys. Acta, 62, 385 (1962).

    Article  CAS  Google Scholar 

  10. Citri, N., and Garber, N., Biochim. Biophys. Acta, 67, 64 (1963).

    Article  CAS  Google Scholar 

  11. Ciba Found. Study Group No. 13: Resistance of Bacteria to the Penicillins, 74 (J. and A. Churchill, Ltd., London, 1962).

  12. Gourevitch, A., Pursiano, T. A., and Lein, J., Nature, 195, 496 (1962).

    Article  ADS  CAS  Google Scholar 

  13. Umbreit, W. W., Burris, R. H., and Stauffer, J. F., Manometric Techniques, 25 (Burgess Publishing Co., Minneapolis, 1957).

    Google Scholar 

Download references

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Authors and Affiliations

  1. Department of Bacteriology, Hebrew University, Hadassah Medical School, Jerusalem

    ELIORA RON-ZENZIPER & NATHAN CITRI

Authors
  1. ELIORA RON-ZENZIPER
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  2. NATHAN CITRI
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RON-ZENZIPER, E., CITRI, N. Modified Substrate Specificity of Cell-bound Penicillinase. Nature 198, 887–888 (1963). https://doi.org/10.1038/198887a0

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