Journal
PARASITOLOGY
Volume 123, Issue -, Pages 33-43Publisher
CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0031182001007946
Keywords
Golgi complex; subcellular fractionation; glycosyltransferases; Trypanosoma cruzi
Categories
Ask authors/readers for more resources
In this study the Golgi complex of the epimastigote forms of Trypanosoma cruzi were isolated and characterized. Using well-controlled sonication to rupture the cells and centrifugation on a discontinuous sucrose density gradient, a highly enriched Golgi fraction was obtained. The Golgi fraction contained most of the beta -galactosyltransferase (beta -Gal transferase) and UDP-N-acetyl-glucosamine: polypeptide-alpha -N-acetyl-glucosaminyltransferase (O-alpha -GlcNAc transferase) activities with minimal contamination of other organelles, as observed by enzymatic assays and electron microscopy analysis. To characterize the Golgi from T. cruzi cells further, it was incubated with a monoclonal antibody against a 58 kDa protein involved in the association of the Golgi complex with microtubules in mammalian cells. Immunofluorescence microscopy showed that the 58 kDa protein is localized in the T. cruzi Golgi region, a result confirmed by high resolution scanning electron microscopy immunocytochemistry. Thus, our results show, for the first time, that the beta -Gal transferase, the alpha -GlcNAc transferase and the 58 kDa protein are present in the Golgi complex of T. cruzi and are novel biochemical markers which can be used in the characterization of this organelle in T. cruzi.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available