Abstract
Sheep hydatid cyst fluid (SHCF) was fractionated on Sephacryl HR S-200 and the anticomplementary activity (α-C activity) determined in the fractions obtained; 67% of total α-C activity of SHCF was recovered in the void volume fraction (SHCF-I) which contained 61% of SHCF carbohydrates. The bulk of the activity of SHCF-I was eluted by FPLC chromatofocusing on Mono P HR at pH 5.9. After heating at 100°C for 15 min, SHCF and SHCF-I conserved 74 and 54%, respectively of their α-C activity. In addition, 37 and 11% of SHCF and SHCF-I α-C activity, respectively bound to Protein A. Components not bound to Protein A (SHCFPA and SHCF-IPA) were fractionated on Con A-Sepharose; 71 and 65%, respectively of their total α-C activity was retained by this lectin indicating the presence of α-D mannoside and α-D glucoside residues in the active molecules. Our results suggest that SHCF could contain two classes of α-C components: immune complexes and thermoresistant molecules with high carbohydrate content.
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