1921
Volume 49, Issue 5
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

The question of whether the African trypanosome utilizes a ubiquitin-ligase system to conjugate the 8,500-dalton protein ubiquitin to other proteins has not been investigated. Using I-labeled ubiquitin and gel electrophoresis (sodium dodecyl sulfate and aceitc acid, urea, Triton X-100), we looked for the incorporation of label into proteins larger than ubiquitin to determine ubiquitin-ligase system activity in cytosolic and nuclear lysates of long slender, intermediate, and short stumpy bloodstream-form trypanosomes. We present data suggesting that there is cytosolic activity of a ubiquitin-ligase system in all three bloodstream forms of . There are indications that the three bloodstream forms of differ in their cytosolic ubiquitin-ligase system activity. Our assay showed no activity of this system in the nucleus of . Further studies on the ubiquitin-ligase system in may define differences between the three bloodstream forms, the parasite, and its host, leading to development of novel chemotherapeutic strategies.

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/content/journals/10.4269/ajtmh.1993.49.545
1993-11-01
2017-11-21
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