Purification and Immuno-Biochemical Characterization of Cattle Hydatid Cyst Fluid Antigen

摘要

In the present study cattle crude hydatid cyst fluid antigen (CCHCFA) was prepared by ammonium sulfateprecipitation, centrifugation and dialysis. Proteins of CCHCFA showed two peaks as PI and P2 when resolvedby gel filtration chromatography on Sephacryl S 200. SDS-PAGE of CCHCFA showed four major polypeptidesof 68 kDa, 22.3 kDa, 15.8 kDa and 8.4 kDa along with two minor polypeptides of 104 kDa and 31.2 kDa. Theinitial part of the ascending loop of the first peak (PI) when resolved by 12.5% SDS-PAGE depicted the welldefined polypeptide of molecular weight of 68 kDa and 61.4 kDa. Double immunodiffusion test, indirect ELISAand western blot analysis demonstrated that the 68 kDa and 61.4 kDa polypeptides were immunoreactive whentreated against hyperimmune sera and known positive sera.