1887

Abstract

The resistance of to amphotericin B methyl ester increases rapidly as cultures enter the stationary phase of growth; organisms harvested after several days in the stationary phase may have a resistance two or three orders of magnitude greater than that of exponentially growing organisms. This resistance is decreased by incubation of the organisms with enzymes which attack components of the cell wall. Of the enzymes tested, (1→3)- -glucanases are the most effective; incubation of 7 d batch cultures with exo-(1→3)--glucanase at a concentration of 10 g enzyme protein (mg dry wt organisms) for 24 h at 37 °C and pH 6·5 reduces the resistance of the organisms to a value approximating to that of exponentially growing organisms. Resistance is also decreased by treatment with chitinase, lipase, trypsin, -mannosidase and (1→6)--glucanases but, on a specific activity basis, none of these enzymes is as effective as (1→3)--glucanase. The action of (1→3)--glucanase is markedly enhanced by the addition during incubation of chitinase, trypsin or lipase.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-117-2-383
1980-04-01
2021-10-15
Loading full text...

Full text loading...

/deliver/fulltext/micro/117/2/mic-117-2-383.html?itemId=/content/journal/micro/10.1099/00221287-117-2-383&mimeType=html&fmt=ahah

References

  1. Cassone A., Kerridge D., Gale E. F. 1979; Ultrastructural changes in the cell wall of Candida albicans following cessation of growth and their possible relationship to the development of polyene resistance.. Journal of General Microbiology 110:339–349
    [Google Scholar]
  2. Davies D. A. L., Pope A. M. S. 1977; Lytic enzymes as antifungal agents - a new approach to antimycotic therapy.. Bulletin of the British Mycological Society 11:144
    [Google Scholar]
  3. Davies D. A. L., Pope A. M. S. 1978; Mycolase, a new kind of systemic antimycotic.. Nature, London 273:235–236
    [Google Scholar]
  4. Gale E. F. 1974; The release of potassium ions from Candida albicans in the presence of polyene antibiotics.. Journal of General Microbiology 80:451–465
    [Google Scholar]
  5. Gale E. F., Johnson A. M., Kerridge D., Koh T. Y. 1975; Factors affecting the changes in amphotericin sensitivity of Candida albicans during growth.. Journal of General Microbiology 87:20–36
    [Google Scholar]
  6. Gale E. F., Johnson A. M., Kerridge D. 1977; The effect of aeration and metabolic inhibitors on resistance to amphotericin in starved cultures of Candida albicans.. Journal of General Microbiology 99:77–84
    [Google Scholar]
  7. Gale E. F., Johnson A. M., Kerridge D., Miles E. A. 1978; Phenotypic resistance to amphotericin B in Candida albicans: the role of reduction.. Journal of General Microbiology 109:191–204
    [Google Scholar]
  8. Glaxo Group Ltd 1966; Preparation of an enzyme complex.. Netherlands Patent appl. 6,506,419 Nov.29, 1965:Chemical Abstracts 65:2972a
    [Google Scholar]
  9. Hammond S. M., Lambert P. A., Kliger B. N. 1974; The mode of action of polyene antibiotics; induced potassium leakage.. Journal of General Microbiology 81:325–330
    [Google Scholar]
  10. Herbert D., Phipps P. J., Strange R. E. 1971; Chemical analysis of microbial cells.. Methods in Microbiology 5B:209344
    [Google Scholar]
  11. Jones G. H., Ballou C. E. 1969; Studies on the structure of yeast mannan 1. Purification and some properties of an α-mannosidase from an Arthrobacter species.. Journal of Biological Chemistry 244:1043–1051
    [Google Scholar]
  12. Marshall J. J. 1972; Facile purification of β glucanhydrolase by chromatography on DEAE-cellulose.. Journal of Chromatography 71:367–385
    [Google Scholar]
  13. Marshall J. J. 1973a; Nature of the binding of a β(l→4) glucanhydrolase to ion exchangers.. Journal of Chromatography 76:257–260
    [Google Scholar]
  14. Marshall J. J. 1973b; Behaviour of β glucanhydrolaseon ion exchangers.. Analytical Chemistry 53:191–198
    [Google Scholar]
  15. Singer T. P., Hofstee B. H. J. 1948; Studies on wheat germ lipase. 1. Methods of estimation, purification and general properties of the enzyme.. Archives of Biochemistry 18:229–259
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-117-2-383
Loading
/content/journal/micro/10.1099/00221287-117-2-383
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