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Mycopathologia

, Volume 131, Issue 2, pp 93–97 | Cite as

Influence of carbon and nitrogen sources on glutathione catabolic enzymes inCandida albicans during dimorphism

  • Suresh Gunasekaran
  • Munyaradzi Imbayagwo
  • Louise McDonald
  • Muthukumaran Gunasekaran
  • Elias Manavathu
Human And Animal Mycology

Abstract

The effect of carbon sources, glucose and sucrose, and nitrogen sources such as ammonia, glutamate andl-citrulline on the activities of glutathione metabolic enzymes has been studied. Yeast and mycelial cells were used to identify changes in activity levels of glutathione reductase (GSSGR), glutathione transferase (GST), glutathione peroxidase (GPX) and γ-glutamyl transpeptidase (GGT). Enzyme activities from cells grown in sucrose media were lower than in glucose media regardless of the enzyme tested, morphological form, or the growth interval. In all enzymes except GST, activity was higher in yeast form than in mycelia, regardless of nitrogen source, with lower activity from 24 to 72 h than at 96 h. In citrulline media, yeast form showed the maximum GST, GGT, and GPX activity. In ammonia-amended media, mycelia showed maximum activity in GGT, whereas in glutamate media, mycelia showed the maximum activity in GST. Also, the type of nitrogen source had no effect on GPX activity in the mycelial form. Finally, changing the nitrogen source showed no significant effect on GSSGR activity, either in the yeast or mycelial form.

Key words

Candida Glutathione Dimorphism Glutathione reductase GlutathioneS-transferase Glutathione peroxidase γ-Glutamyl transpeptidase 

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Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Suresh Gunasekaran
    • 1
  • Munyaradzi Imbayagwo
    • 1
  • Louise McDonald
    • 2
  • Muthukumaran Gunasekaran
    • 1
  • Elias Manavathu
    • 2
  1. 1.Department of BiologyFisk UniversityNashvilleUSA
  2. 2.Department of MedicineWayne State UniversityDetroitUSA

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