Trypanosoma rhodesiense: Mitochondrial proteins of bloodstream and procyclic trypomastigotes

Rance B Lefebvre, George C. Hill

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

One- and two-dimensional gel electrophoresis of the solubilized mitochondrial proteins of bloodstream and procyclic trypomastigote Trypanosoma brucei rhodesiense and radiolabeling of proteins in the presence of cycloheximide were used to identify proteins synthesized in the trypanosome mitochondrion. The proteins which comprise the mitochondrion were found to be very similar in both bloodstream and procyclic trypomastigotes, but do differ in their level of synthesis. A protein putatively identified as subunit II of cytochrome oxidase (EC 1.9.3.1) was detected in mitochondria from both the procyclic and bloodstream organisms. The presence of this protein in bloodstream trypomastigotes and the overall similarity of protein content in the trypanosome mitochondria is noteworthy in view of the fact that bloodstream trypomastigotes have a repressed mitochondrion with no detectable tricarboxylic acid cycle or cytochrome electron transport chain.

Original languageEnglish (US)
Pages (from-to)85-91
Number of pages7
JournalExperimental Parasitology
Volume62
Issue number1
DOIs
StatePublished - 1986
Externally publishedYes

Keywords

  • Cycloheximide
  • Cytochrome oxidase (EC 1.9.3.7)
  • Hemoflagellate
  • Mitochondria
  • Proteins
  • Protozoa, parasitic
  • Trypanosoma brucei rhodesiense

ASJC Scopus subject areas

  • Immunology
  • Parasitology
  • Infectious Diseases

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