Abstract
The study focused on purification, characterization and isolation of excretory/secretory antigens of ovine paramphistomes. A total of 5.321 and 7.170 mg of protein was obtained from 630 adult Cotylophoron cotylophorum and 290 adults Gastrothylax crumenifer, respectively. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) (12%) analysis of purified C. cotylophrum revealed 6 polypeptides in the range of 10 to 35 kDa while a prominent band at 15 kDa with G. crumenifer. Western blot analysis of purified excretory/secretory antigens of C. cotylophorum revealed 4 immuno-determinant bands in the range of 10 to 30 kDa using their specific rabbit hyperimmune serum, whereas G. crumenifer showed 2 polypeptides between 10 to 25 kDa. The common polypeptide observed at 20 kDa in both purified excretory/secretaty antigens can be used as a candidate antigen for development of serodiagnosis in the early stage of infection.
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