Preliminary characterization of anticomplementary components of hydatid cyst fluid.
Sheep hydatid cyst fluid (SHCF) was fractionated on Sephacryl HR S-200 and the anticomplementary activity (alpha-C activity) determined in the fractions obtained; 67% of total alpha-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 degrees C for 15 min, SHCF and SHCF-I conserved 74 and 54%, respectively of their alpha-C activity. In addition, 37 and 11% of SHCF and SHCF-I alpha-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 alpha-C activity was retained by this lectin indicating the presence of alpha-D mannoside and alpha-D glucoside residues in the active molecules. Our results suggest that SHCF could contain two classes of alpha-C components: immune complexes and thermoresistant molecules with high carbohydrate content.
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Cátedra de Inmunología, Facultad de Química, Instituto de Higiene, Montevideo, Uruguay.
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D000818:Animals; D003169:Complement Inactivator Proteins / Q000032:analysis* / Q000737:chemistry; D003165:Complement System Proteins / Q000276:immunology*; D004443:Echinococcosis / Q000276:immunology / Q000662:veterinary*; D012756:Sheep; D012757:Sheep Diseases / Q000276:immunology*
D003169:Complement Inactivator Proteins; D003165:Complement System Proteins