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. 1982 Nov;152(2):567–571. doi: 10.1128/jb.152.2.567-571.1982

Characterization of eight beta-lactamases of Gram-negative bacteria.

T Sawai, M Kanno, K Tsukamoto
PMCID: PMC221503  PMID: 6752115

Abstract

Eight kinds of beta-lactamases produced by gram-negative bacteria were characterized by the following properties: molecular weight, isoelectric point, pH optimum, molecular activity, immunochemical reactivity, and kinetic parameters with respect to twelve kinds of common beta-lactam antibiotics. These beta-lactamases included two types of penicillinases mediated by R plasmids and six kinds of species-specific cephalosporinases. To determine a reliable value of the kinetic parameter, Km, we introduced a continuous and acidimetric assay method of beta-lactamase activity with a pH stat.

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Selected References

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  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. Fujii-Kuriyama Y., Yamamoto M., Sugawara S. Purification and properties of beta-lactamase from Proteus morganii. J Bacteriol. 1977 Sep;131(3):726–734. doi: 10.1128/jb.131.3.726-734.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fukagawa Y., Takei T., Ishikura T. Inhibition of beta-lactamase of Bacillus licheniformis 749/C by compound PS-5, a new beta-lactam antibiotic. Biochem J. 1980 Jan 1;185(1):177–185. doi: 10.1042/bj1850177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. IMSANDE J. NEW ASSAY FOR PENICILLINASE AND SOME RESULTS ON PENICILLINASE INDUCTION. J Bacteriol. 1965 May;89:1322–1327. doi: 10.1128/jb.89.5.1322-1327.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Labia R., Andrillon J., Le Goffic F. Computerized microacidimetric determination of beta lactamase Michaelis-Menten constants. FEBS Lett. 1973 Jun 15;33(1):42–44. doi: 10.1016/0014-5793(73)80154-1. [DOI] [PubMed] [Google Scholar]
  8. Le Goffic F., Andrillon-Spiegel J., Letarte R. Immunogical study of anti-beta-lactamase antibodies by acidimetric methods. Antimicrob Agents Chemother. 1974 Dec;6(6):676–679. doi: 10.1128/aac.6.6.676. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Matsubara N., Yotsuji A., Kumano K., Inoue M., Mitsuhashi S. Purification and some properties of a cephalosporinase from Proteus vulgaris. Antimicrob Agents Chemother. 1981 Jan;19(1):185–187. doi: 10.1128/aac.19.1.185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. REISFELD R. A., LEWIS U. J., WILLIAMS D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature. 1962 Jul 21;195:281–283. doi: 10.1038/195281a0. [DOI] [PubMed] [Google Scholar]
  12. Rubin F. A., Smith D. H. Characterization of R factor beta-lactamases by the acidimetric method. Antimicrob Agents Chemother. 1973 Jan;3(1):68–73. doi: 10.1128/aac.3.1.68. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sawai T., Mitsuhashi S., Yamagishi S. Drug resistance of enteric bacteria. XIV. Comparison of beta-lactamases in gram-negative rod bacteria resistant to alpha-aminobenzylpenicillin. Jpn J Microbiol. 1968 Dec;12(4):423–434. doi: 10.1111/j.1348-0421.1968.tb00415.x. [DOI] [PubMed] [Google Scholar]
  14. Sawai T., Nakajima S., Morohoshi T., Yamagishi S. Thermolabile repression of cephalosporinase synthesis in Citrobacter freundii. Microbiol Immunol. 1977 Nov;21(11):631–638. doi: 10.1111/j.1348-0421.1977.tb00331.x. [DOI] [PubMed] [Google Scholar]
  15. Sawai T., Takahashi I., Nakagawa H., Yamagishi S. Immunochemical comparison between an oxacillin-hydrolyzing penicillinase of Aeromonas hydrophila and those mediated by R plasmids. J Bacteriol. 1978 Jul;135(1):281–282. doi: 10.1128/jb.135.1.281-282.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sawai T., Takahashi I., Yamagishi S. Iodometric assay method for beta-lactamase with various beta-lactam antibiotics as substrates. Antimicrob Agents Chemother. 1978 Jun;13(6):910–913. doi: 10.1128/aac.13.6.910. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sawai T., Takahashi K., Yamagishi S., Mitsuhashi S. Variant of penicillinase mediated by an R factor in Escherichia coli. J Bacteriol. 1970 Nov;104(2):620–629. doi: 10.1128/jb.104.2.620-629.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sawai T., Yamagishi S., Mitsuhashi S. Penicillinases of Klebsiella pneumoniae and their phylogenetic relationship to penicillinases mediated by R factors. J Bacteriol. 1973 Sep;115(3):1045–1054. doi: 10.1128/jb.115.3.1045-1054.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sawai T., Yoshida T. A simple method for testing the efficacy of a beta-lactamase inhibitor against beta-lactamase-producing gram-negative bacteria. J Antibiot (Tokyo) 1982 Aug;35(8):1072–1077. doi: 10.7164/antibiotics.35.1072. [DOI] [PubMed] [Google Scholar]
  20. Sawai T., Yoshida T., Tsukamoto K., Yamagishi S. A set of bacterial strains for evaluation of beta-lactamase-stability of beta-lactam antibiotics. J Antibiot (Tokyo) 1981 Oct;34(10):1318–1326. doi: 10.7164/antibiotics.34.1318. [DOI] [PubMed] [Google Scholar]
  21. Takahashi I., Sawai T., Ando T., Yamagishi S. Cefoxitin resistance by a chromosomal cephalosporinase in Escherichia coli. J Antibiot (Tokyo) 1980 Sep;33(9):1037–1042. doi: 10.7164/antibiotics.33.1037. [DOI] [PubMed] [Google Scholar]
  22. Yun S. L., Suelter C. H. A simple method for calculating Km and V from a single enzyme reaction progress curve. Biochim Biophys Acta. 1977 Jan 11;480(1):1–13. doi: 10.1016/0005-2744(77)90315-1. [DOI] [PubMed] [Google Scholar]

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