1887

Abstract

SUMMARY: Two -lactamases, A and B, have been shown to be present in a strain of (W222). -Lactamase A hydrolyses a variety of penicillins and cephalosporins. This enzyme is sensitive to thiol reagents, is only partially inhibited 0·1 m-cloxacillin and has a molecular weight of approximately 20000. -Lactamase B shows strong cephalosporinase activity but does not hydrolyse some of the penicillins. It is more resistant than -lactamase A to thiol reagents, is completely inhibited 0·1 m-cloxacillin and has a molecular weight of about 34000. With cephaloridine as a substrate, which is readily hydrolysed both enzymes, about 85% of the total activity of a cell extract is due to -lactamase A and 15% to B. Addition of 6-aminopenicillanic acid to the culture during growth results in a 2- to 4-fold selective increase in the amount of -lactamase B. Two -lactamases similar to enzymes A and B have been found in five other strains of In contrast, only one -lactamase, similar to enzyme B, has been detected in a different strain of (H66), which is abnormal in that it is sensitive to ampicillin. Addition of 6-aminopenicillanic acid to cultures of this strain results in an 8- to 10-fold increase in -lactamase production.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-87-2-273
1975-04-01
2021-10-16
Loading full text...

Full text loading...

/deliver/fulltext/micro/87/2/mic-87-2-273.html?itemId=/content/journal/micro/10.1099/00221287-87-2-273&mimeType=html&fmt=ahah

References

  1. Andrews P. 1964; Estimation of the molecular weight of proteins by Sephadex gel filtration. Biochemical Journal 91:222–233
    [Google Scholar]
  2. Ayliffe G. A. J. 1964; Induction of cephalosporinase and penicillinase in Proteus species. Nature; London: 2011032
    [Google Scholar]
  3. Ayliffe G. A. J. 1965; Cephalosporinase and penicillinase activity of Gram-negative bacteria. Journal of General Microbiology 40:119–126
    [Google Scholar]
  4. Cornelis G., Wauters G., Bruynoghe G. 1973a; Resistances transferables chez des souches sauvages de Yersinia enterocolitica. Annales de Microbiologie (Institut Pasteur) 124A:299–309
    [Google Scholar]
  5. Cornelis G., Wauters G., Vanderhaeghe H. 1973b; Presence de β-lactamase chez Yersinia entero-colitica. Annales de Microbiologie {Institut Pasteur) 124B:139–152
    [Google Scholar]
  6. Crompton B., Jago M., Crawford K., Newton G. G. F., Abraham E. P. 1962; Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicilIanic acid as substrates, inhibitors and inducers of penicillinases. Biochemical Journal 83:52–63
    [Google Scholar]
  7. Eadie G. S. 1942; The inhibition of cholinesterase by physostigmine and prostigmine. Journal of Biological Chemistry 146:85–93
    [Google Scholar]
  8. Eykyn S., Jenkins C., King A., Phillips I. 1973; Antibacterial activity of cefamandole, a new cephalosporin antibiotic, compared with that of cephaloridine, cephalothin, and cephalexin. Antimicrobial Agents and Chemotherapy 3:657–661
    [Google Scholar]
  9. Habeeb A. F. S. A. 1972; Reaction of protein sulphydryl groups with Ellman’s reagent. Methods in Enzymology 25:457–464
    [Google Scholar]
  10. Hennessey T. D. 1967; Inducible β-lactamase in Enterobacter. Journal of General Microbiology 49:277–285
    [Google Scholar]
  11. Hou J. P., Poole J. W. 1972; Measurement of β-lactamase activity and rate of inactivation of penicillins by a pH-stat alkalimetric titration method. Journal of Pharmaceutical Sciences 61:1594–1598
    [Google Scholar]
  12. Jack G. W., Richmond M. H. 1970; A comparative study of eight distinct β-lactamases synthesized by Gram-negative bacteria. Journal of General Microbiology 61:43–61
    [Google Scholar]
  13. Mcphail M., Furth A. 1973; Purification and properties of an inducible β-lactamase from Pseudomonas aeruginosa n.c.t.c. 8203. Biochemical Society Transactions 1:1260–1263
    [Google Scholar]
  14. Mishankin B. N., Ryzhko I. V., Grigorian E. G. 1973; Study of penicillinase activity of Pasteurella pseudotuberculosis and Pasteurella X. Antibiotiki 18:621–624
    [Google Scholar]
  15. Newsom S. W. B., Sykes R. B., Richmond M. H. 1970; Detection of a β-lactamase markedly active against carbenicillin in a strain of Pseudomonas aeruginosa. Journal of Bacteriology 101:1079–1080
    [Google Scholar]
  16. Niléhn B. 1967; Studies on Yersinia enterocolitica. Acta pathologica et microbiologica scandinavica 69:83–91
    [Google Scholar]
  17. Niléhn B. 1969; Studies on Yersinia enterocolitica: with special reference to bacterial diagnosis and occurrence in human acute enteric disease. Acta pathologica et microbiologica scandinavica 206:1–48
    [Google Scholar]
  18. Novick R. P. 1962; Micro-iodometric assay for penicillinase. Biochemical Journal 83:236–240
    [Google Scholar]
  19. O’Callaghan C. H., Morris A., Kirby S. M., Shingler A. H. 1972; Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrobial Agents and Chemotherapy 1:283–288
    [Google Scholar]
  20. Richmond M. H., Jack G. W., Sykes R. B. 1971; The β-lactamases of Gram-negative bacteria including pseudomonads. Annals of the New York Academy of Sciences 182:243–257
    [Google Scholar]
  21. Sabath L. D., Abraham E. P. 1966; Zinc as a cofactor for cephalosporinase from Bacillus cereus 569. Biochemical Journal 98:11C–13C
    [Google Scholar]
  22. Sabath L. D., Jago M., Abraham E. P. 1965; Cephalosporinase and pencillinase activities of a β-lactamase from Pseudomonas pyocyanae. Biochemical Journal 96:739–752
    [Google Scholar]
  23. Smith J. T. 1963; Sulphydryl groups essential for the penicillinase activity of Aerobacter cloacae. Nature; London: 197900–901
    [Google Scholar]
  24. Smith B., Warren S. G., Newton G. G. F., Abraham E. P. 1967; Biosynthesis of penicillin N and cephalosporin C. Biochemical Journal 103:877–890
    [Google Scholar]
  25. Waley S. G. 1974; Report on a spectrophotometric assay of β-lactamase activity on penicillins. Biochemical Journal 139:789–790
    [Google Scholar]
  26. Wauters G. 1970 Contribution a l’etude de Yersinia enterocolitica pp. 13–15 Thesis University of Louvain; Vander. Edited by
    [Google Scholar]
  27. Wauters G., Le Minor L., Chalon A. M. 1971; Antigenes somatiques et flagellaires des Yersinia enterocolitica. Annales de l’Institut Pasteur 120:631–642
    [Google Scholar]
  28. Wauters G., Le Minor L., Chalon A. M., Lassen J. 1972; Supplement au schema antigenique de Yersinia enterocolitica. Annales de l’Institut Pasteur 122:951–956
    [Google Scholar]
  29. Winblad S. 1967; Studies on serological typing of Yersinia enterocolitica. Acta pathologica et micro-biologica scandinavica S187:115
    [Google Scholar]
  30. Winblad S. 1968; Studies on O antigen factors of Y. enterocolitica. In International Symposium on Pseudotuberculosis 1968 Symposia Series in Immunobiological Standardization 9 pp. 337–342 Basle: Karger;
    [Google Scholar]
  31. Winblad S., Niléhn B., Sternby N. H. 1966; Yersinia enterocolitica (Pasteurella X) in human enteric infections. British Medical Journal 2:1363–1366
    [Google Scholar]
  32. Yaginuma S., Sawai T., Ono H., Yamagishi S., Mitsuhashi S. 1973; Biochemical properties of a cephalosporin β-lactamase from Pseudomonas aeruginosa. Japanese Journal of Microbiology 17:141–149
    [Google Scholar]
  33. Zyk N., Kalkstein A., Citri N. 1972; Purification and properties of a β-lactamase of Pseudomonas aeruginosa. Israel Journal of Medicine 8:1906–1911
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-87-2-273
Loading
/content/journal/micro/10.1099/00221287-87-2-273
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error