| Literature DB >> 16222528 |
S C Yadav1, M Saini, O K Raina, P A Nambi, K Jadav, D Sriveny.
Abstract
Cathepsin-L cysteine proteinase was purified from Fasciola gigantica regurgitant by two-step alcoholic fractionation, followed by ion-exchange chromatography. The purification strategy was evolved to eliminate other contaminating proteins co-precipitating with the purified proteinase during alcoholic fractionation. The enzyme was stable on long-term storage at -20 degrees C rendering it more suitable for field diagnostic use. The purified cathepsin-L cysteine proteinase was assayed for detection of F. gigantica experimental infection in sheep and buffaloes and could detect infection, as early as 4 weeks post-infection by ELISA, Western blotting and Dipstick ELISA. The 28-kDa cathepsin-L cysteine proteinase seems a promising antigen for the diagnosis of tropical fasciolosis in domestic animals.Entities:
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Year: 2005 PMID: 16222528 DOI: 10.1007/s00436-005-1466-8
Source DB: PubMed Journal: Parasitol Res ISSN: 0932-0113 Impact factor: 2.289