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http://nopr.niscpr.res.in/handle/123456789/15387| Title: | Purification and characterization of a cholinesterase from Haemonchus contortus |
| Authors: | Joshi, P Singh, B P |
| Issue Date: | Jun-2000 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | Acetylcholinesterase (AChE) was purified from the extract of adult Haemonchus contortus by gel filtration, ion-exchange and ConA-Sepharose chromatography. The enzyme was also found to be secreted by the parasite during in vitro cultivation which was partially purified from the excretory-secretory products. Presence of enzyme specific antibodies were observed in animals having H. contortus infection. The molecular mass of the enzyme by SDS-PAGE was 144 kDa. The enzyme showed typical Michaelis-Menten kinetics at low substrate concentrations but was inhibited by substrate concentrations greater than 4 mM. The enzyme was stab le at 4°C for several weeks but lost 60% of the activity when heated to 60°C for 5 min. Physostigmine and neostigmine inhibited enzyme activity at low ( μM) concentrations whereas phenyl methyl sulfonyl fluoride (PMSF) and sodium fluoride (NaF) inhibited only at high concentrations (mM) . Significance of secreted AChE in host-parasite relationship is discussed. |
| Page(s): | 192-197 |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Appears in Collections: | IJBB Vol.37(3) [June 2000] |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| IJBB 37(3) 192-197.pdf | 1.28 MB | Adobe PDF | View/Open |
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