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. 1994;80(4):336-41.
doi: 10.1007/BF02351876.

Glycolipid and protein profiles in trypanosomatids

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Glycolipid and protein profiles in trypanosomatids

M H Branquinha et al. Parasitol Res. 1994.

Abstract

A comparative study of glycolipid and protein composition in Trypanosoma cruzi and non-pathogenic trypanosomatids was carried out using Triton X-114 extraction. Protein profiles were analysed by polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS-PAGE), and glycolipids were detected using high-performance thin-layer chromatography (HPTLC). Hydrophilic protein profiles were similar in non-pathogenic protozoa. Endotrypanum schaudinni, Crithidia luciliae and T. mega showed five characteristic protein bands ranging between 30 and 66 kDa. In the hydrophobic phase, a band of 50 kDa was present only in T. mega. Strain-specific protein distribution was detected in T. cruzi clone Dm28c and T. cruzi G and Y strains; clone Dm28c had five typical hydrophilic proteins at between 24 and 45 kDa, the G strain had two bands at 45 kDa in the hydrophilic phase and the Y strain had a major protein band at 24 kDa in both phases. T. dionisii and T. cruzi clone Dm28c showed a characteristic distribution of three hydrophilic proteins of approx. 45 kDa. Qualitative analysis of glycolipid composition showed that the T. cruzi strains and Dm28c clone and T. dionisii had four orcinol-positive spots, whereas in the other non-pathogenic trypanosomatids only three glycolipids were detected.

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