Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1968 Sep;109(3):469–473. doi: 10.1042/bj1090469

The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae

T D Hennessey 1,2,*, M H Richmond 1,2
PMCID: PMC1186840  PMID: 5685878

Abstract

1. A β-lactamase has been purified from a strain of Enterobacter cloacae. 2. This enzyme is about eighty times as active against cephaloridine as against benzylpenicillin or ampicillin. 3. The enzyme has a net positive charge at pH8·0 and a molecular weight of about 14000. 4. An approximate amino acid composition of the enzyme is reported.

Full text

PDF
469

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambler R. P., Brown L. H. The amino acid sequence of Pseudomonas fluorescens azurin. Biochem J. 1967 Sep;104(3):784–825. doi: 10.1042/bj1040784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Citri N., Pollock M. R. The biochemistry and function of beta-lactamase (penicillinase). Adv Enzymol Relat Areas Mol Biol. 1966;28:237–323. doi: 10.1002/9780470122730.ch4. [DOI] [PubMed] [Google Scholar]
  3. Datta N. Infectious drug resistance. Br Med Bull. 1965 Sep;21(3):254–259. doi: 10.1093/oxfordjournals.bmb.a070405. [DOI] [PubMed] [Google Scholar]
  4. Datta N., Kontomichalou P. Penicillinase synthesis controlled by infectious R factors in Enterobacteriaceae. Nature. 1965 Oct 16;208(5007):239–241. doi: 10.1038/208239a0. [DOI] [PubMed] [Google Scholar]
  5. Datta N., Richmond M. H. The purification and properties of a penicillinase whose synthesis is mediated by an R-factor in Escherichia coli. Biochem J. 1966 Jan;98(1):204–209. doi: 10.1042/bj0980204. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FLEMING P. C., GOLDNER M., GLASS D. G. Observations on the nature, distribution, and significance of cephalosporinase. Lancet. 1963 Jun 29;1(7296):1399–1401. doi: 10.1016/s0140-6736(63)92051-8. [DOI] [PubMed] [Google Scholar]
  7. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  8. Hamilton-Miller J. M., Smith J. T., Knox R. Interaction of cephaloridine with penicillinase-producing gram-negative bacteria. Nature. 1965 Oct 16;208(5007):235–237. doi: 10.1038/208235a0. [DOI] [PubMed] [Google Scholar]
  9. Hennessey T. D. Inducible beta-lactamase in Enterobacter. J Gen Microbiol. 1967 Nov;49(2):277–285. doi: 10.1099/00221287-49-2-277. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. NOVICK R. P. Micro-iodometric assay for penicillinase. Biochem J. 1962 May;83:236–240. doi: 10.1042/bj0830236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. PERRET C. J. Iodometric assay of penicillinase. Nature. 1954 Nov 27;174(4439):1012–1013. doi: 10.1038/1741012a0. [DOI] [PubMed] [Google Scholar]
  13. POLLOCK M. R., TORRIANI A. M. Purification et caractéristiques physicochimiques de la pénicillinase de Bacillus cereus. C R Hebd Seances Acad Sci. 1953 Jul 20;237(3):276–278. [PubMed] [Google Scholar]
  14. SMITH J. T., HAMILTON-MILLER J. M. Differences between pencillinases from gram-positive and gram-negative bacteria. Nature. 1963 Mar 9;197:976–978. doi: 10.1038/197976a0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES