| Literature DB >> 3026835 |
Abstract
The first six glycolytic enzymes in epimastigote Trypanosoma cruzi were shown to behave similarly during differential centrifugation, when maximum relative specific activity was found in the small granule fraction, and by isopycnic centrifugation, when the bulk of each activity coequilibrated on sucrose gradients with a modal density of 1.23 g/ml. All six showed substantial detergent latency in whole cell homogenates. Electron microscopic examination of fractions from a sucrose gradient with modal density 1.23 g/ml showed the presence of single membrane bound vesicles of diameter 0.2-0.8 micron. It was concluded that these six enzymes were contained in a microbodylike organelle, termed the "glycosome." Phosphoglucose isomerase (EC 5.3.1.9) also possessed substantial soluble activity. No microbody marker enzyme described in other sources could be detected. Peroxidase (EC 1.11.1.7) had an insignificant glycosomal component. Enzymes of amino acid and fatty acid metabolism were not detected in microbody fractions. Marker enzymes for the flagellar pocket and plasma membrane were suggested.Entities:
Mesh:
Substances:
Year: 1987 PMID: 3026835 DOI: 10.1016/0014-4894(87)90081-6
Source DB: PubMed Journal: Exp Parasitol ISSN: 0014-4894 Impact factor: 2.011