PURIFICATION AND IMMUNO-BIOCHEMICAL CHARACTERIZATION OF CATTLE HYDATID CYST FLUID ANTIGEN

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