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Lactate dehydrogenase in two digenetic trematodes and their host
M Haque1, A H Siddiqi, J Siddiqui
1Department of Zoology, Aligarh Muslim University, India.
International Journal for Parasitology
|December 1, 1990
Summary
Researchers compared lactate dehydrogenase (LDH) isoenzymes in water buffalo parasites and host tissues. Parasitic LDH showed distinct characteristics, including different thiol inhibitor susceptibility and lower heat stability compared to host LDH.
Area of Science:
- Biochemistry
- Parasitology
- Veterinary Science
Background:
- Digenetic trematodes Gigantocotyle explanatum and Gastrothylax crumenifer infect water buffalo.
- Lactate dehydrogenase (LDH) is a crucial enzyme in cellular metabolism.
- Understanding enzyme differences between parasites and hosts is vital for control strategies.
Purpose of the Study:
- To characterize and compare lactate dehydrogenase (LDH) isoenzymes in two digenetic trematodes and their water buffalo host tissues.
- To investigate the biochemical properties and inhibitor susceptibility of parasitic and host LDH.
Main Methods:
- Polyacrylamide gel electrophoresis (PAGE) was used to separate LDH isoenzymes.
- Spectrophotometric analysis assessed enzyme activity and inhibitor effects.
- Thermal stability assays were performed.
Main Results:
- Six and seven LDH isoenzymes were detected in Gigantocotyle explanatum and Gastrothylax crumenifer, respectively.
- Five host-specific LDH isoenzymes were identified in water buffalo liver and rumen tissues.
- Parasitic and host LDH exhibited differential susceptibility to parachloromercuribenzoate and iodoacetate.
- Parasitic LDH showed lower thermal stability than host LDH.
Conclusions:
- Significant biochemical differences exist in LDH isoenzymes between the parasites and their host.
- These enzymatic distinctions may offer targets for developing antiparasitic interventions.
- LDH characterization provides insights into host-parasite metabolic interactions.