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. 1990 Feb;34(2):349–354. doi: 10.1128/aac.34.2.349

In vitro investigation of BK-218, a new oral and parenteral cephalosporin.

I Szabó 1, J Barabás 1, A Tar 1, L Kiss 1, M Filep 1, T Schmidt 1, K Marossy 1, B Tóth-Martinez 1, G Barabás 1, F Hernádi 1
PMCID: PMC171585  PMID: 2109582

Abstract

The antibacterial activity of BK-218 was similar to that of cefamandole when it was tested against several laboratory strains. The inhibiting effect of BK-218 was greater than that of cephalexin and cefoxitin on penicillin-binding proteins of Escherichia coli HB101. This result was in close correlation with the relative inhibition of radiolabeled glucosamine incorporation (greatest with BK-218) and with the lytic effect (most intensive with BK-218). BK-218 proved to be a good inhibitor for all five of the beta-lactamases that were investigated, although two enzymes (Enterobacter cloacae P99 and Pseudomonas aeruginosa Cilote) hydrolyzed it to some extent.

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Selected References

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

  1. ABRAHAM E. P., NEWTON G. G. Experiments on the degradation of cephalosporin C. Biochem J. 1956 Apr;62(4):658–665. doi: 10.1042/bj0620658. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Berks M., Redhead K., Abraham E. P. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa. J Gen Microbiol. 1982 Jan;128(1):155–159. doi: 10.1099/00221287-128-1-155. [DOI] [PubMed] [Google Scholar]
  3. Bill N. J., Washington J. A., 2nd Comparison of in vitro activity of cephalexin, cephradine, and cefaclor. Antimicrob Agents Chemother. 1977 Mar;11(3):470–474. doi: 10.1128/aac.11.3.470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  5. Boyer H. W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. doi: 10.1016/0022-2836(69)90288-5. [DOI] [PubMed] [Google Scholar]
  6. Buck R. E., Price K. E. Cefadroxil, a new broad-spectrum cephalosporin. Antimicrob Agents Chemother. 1977 Feb;11(2):324–330. doi: 10.1128/aac.11.2.324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cartwright S. J., Waley S. G. Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose. Biochem J. 1984 Jul 15;221(2):505–512. doi: 10.1042/bj2210505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cartwright S. J., Waley S. G. beta-Lactamase inhibitors. Med Res Rev. 1983 Oct-Dec;3(4):341–382. doi: 10.1002/med.2610030402. [DOI] [PubMed] [Google Scholar]
  9. Coyette J., Ghuysen J. M., Binot F., Adriaens P., Meesschaert B., Vanderhaeghe H. Interactions between beta-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790. Eur J Biochem. 1977 May 2;75(1):231–239. doi: 10.1111/j.1432-1033.1977.tb11522.x. [DOI] [PubMed] [Google Scholar]
  10. De Boer W. R., Kruyssen F. J., Wouters J. T. Cell wall turnover in batch and chemostat cultures of Bacillus subtilis. J Bacteriol. 1981 Jan;145(1):50–60. doi: 10.1128/jb.145.1.50-60.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fontana R., Canepari P., Satta G., Coyette J. Identification of the lethal target of benzylpenicillin in Streptococcus faecalis by in vivo penicillin binding studies. Nature. 1980 Sep 4;287(5777):70–72. doi: 10.1038/287070a0. [DOI] [PubMed] [Google Scholar]
  12. Kiener P. A., Waley S. G. Reversible inhibitors of penicillinases. Biochem J. 1978 Jan 1;169(1):197–204. doi: 10.1042/bj1690197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kiss L., Tar A., Gál S., Toth-Mortinez B. L., Hernádi F. J. Modified general affinity adsorbent for large-scale purification of penicillinases. J Chromatogr. 1988 Aug 31;448(1):109–116. doi: 10.1016/s0021-9673(01)84569-6. [DOI] [PubMed] [Google Scholar]
  14. Kitano K., Tomasz A. Triggering of autolytic cell wall degradation in Escherichia coli by beta-lactam antibiotics. Antimicrob Agents Chemother. 1979 Dec;16(6):838–848. doi: 10.1128/aac.16.6.838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Labia R., Guionie M., Barthélémy M. Properties of three carbenicillin-hydrolysing beta-lactamases (CARB) from Pseudomonas aeruginosa: identification of a new enzyme. J Antimicrob Chemother. 1981 Jan;7(1):49–56. doi: 10.1093/jac/7.1.49. [DOI] [PubMed] [Google Scholar]
  16. Labia R., Guionie M., Masson J. M., Philippon A., Barthelemy M. Beta-lactamases produced by a Pseudomonas aeruginosa strain highly resistant to carbenicillin. Antimicrob Agents Chemother. 1977 May;11(5):785–790. doi: 10.1128/aac.11.5.785. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  18. Neu H. C., Fu K. P. Cefaclor: in vitro spectrum of activity and beta-lactamase stability. Antimicrob Agents Chemother. 1978 Apr;13(4):584–588. doi: 10.1128/aac.13.4.584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Neu H. C., Fu K. P. Cefatrizine activity compared with that of other cephalosporins. Antimicrob Agents Chemother. 1979 Feb;15(2):209–212. doi: 10.1128/aac.15.2.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. O'Callaghan C. H., Morris A., Kirby S. M., Shingler A. H. Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother. 1972 Apr;1(4):283–288. doi: 10.1128/aac.1.4.283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pooley H. M. Layered distribution, according to age, within the cell wall of bacillus subtilis. J Bacteriol. 1976 Mar;125(3):1139–1147. doi: 10.1128/jb.125.3.1139-1147.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Samuni A. A direct spectrophotometric assay and determination of Michaelis constants for the beta-lactamase reaction. Anal Biochem. 1975 Jan;63(1):17–26. doi: 10.1016/0003-2697(75)90185-2. [DOI] [PubMed] [Google Scholar]
  23. Sawai T., Kanno M., Tsukamoto K. Characterization of eight beta-lactamases of Gram-negative bacteria. J Bacteriol. 1982 Nov;152(2):567–571. doi: 10.1128/jb.152.2.567-571.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Simpson I. N., Plested S. J., Harper P. B. Investigation of the beta-lactamase stability of ceftazidime and eight other new cephalosporin antibiotics. J Antimicrob Chemother. 1982 May;9(5):357–368. doi: 10.1093/jac/9.5.357. [DOI] [PubMed] [Google Scholar]
  25. Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
  26. Sykes R. B. The classification and terminology of enzymes that hydrolyze beta-lactam antibiotics. J Infect Dis. 1982 May;145(5):762–765. doi: 10.1093/infdis/145.2.762. [DOI] [PubMed] [Google Scholar]
  27. Then R. L., Angehrn P. Trapping of nonhydrolyzable cephalosporins by cephalosporinases in Enterobacter cloacae and Pseudomonas aeruginosa as a possible resistance mechanism. Antimicrob Agents Chemother. 1982 May;21(5):711–717. doi: 10.1128/aac.21.5.711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Toth-Martinez B. L., Gál S., Kiss L. Chromatofocusing for separation of beta-lactamases. I. Microscale separation of RTEM- and chromosomally mediated beta-lactamases of Escherichia coli J6-2. J Chromatogr. 1983 Jun 24;262:373–378. doi: 10.1016/s0021-9673(01)88123-1. [DOI] [PubMed] [Google Scholar]
  29. Waley S. G. A spectrophotometric assay of beta-lactamase action on penicillins. Biochem J. 1974 Jun;139(3):789–790. doi: 10.1042/bj1390789. [DOI] [PMC free article] [PubMed] [Google Scholar]

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