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A histochemical assay was elaborated to study lactate dehydrogenase activity in the tissues of Fasciola hepatica and in the liver of mice during the course of fasciolosis. LDH activity was determined in the tegument, muscles, parenchyma, oral sucker and the caecum of juvenile and adult liver flukes inhabiting the host liver parenchyma and bile ducts. The most substantial changes in LDH activity were recorded in the tegument outer surface layer. White mice of CFW strain were infected with 10, 30 and 50 doses of F. hepatica metacerkariae administered per os. A dramatic decrease in LDH activity in the experimental mice liver during the course of infection, particularly in the acute fasciolosis was observed.
CFW strain white mice were infected with various doses (10, 30, 50 and 100) of Fasciola hepatica metacercariae administered per os. Using histochemical methods, the activity of selected oxidoreductases (α-glycerophosphate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, and cytochrome oxidase) was evaluated in the liver of the mice suffering from acute and chronic fasciolosis. Intensified anaerobic and aerobic respiration was recorded. The host’s compensatory mechanism observed in the form of intensified metabolism, was found to be related to the infection intensity.
Histochemical assays were made to study the activity of the following respiratory enzymes: α-glycerophosphate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, and cytochrome oxidase in tissues of Fasciola hepatica during the parasite’s development in the liver of the definitive host. The respiratory enzyme activity was assessed in the tegument, parenchyma, oral sucker, and in the caecum of juvenile and adult F. hepatica inhabiting the host’s liver parenchyma (infection week 1 to 4) and bile ducts (infection week 5-7), respectively. Changes in the intensity of the parasite’s reaction to the dehydrogenases studied were found to be habitat-dependent (liver parenchyma vs. bile ducts). No cytochrome oxidase activity was detected in F. hepatica tissues.
The localisation and activity of D glucose-6-phosphatase (G-6-Pase) and alkaline phosphatase (AlP) in the trophozoites of Balantidium coli isolated from pig intestine content were investigated using ultrastructural and cytochemical methods. The activity of G-6-Pase was demonstrated on the membranes of the endoplasmic reticulum, particularly in the cortical part of the trophozoites. In addition, the product of the reaction to G-6-Pase was concentrated in the vesicular structures, which were distributed along the reticular membranes. These structures were described as vesicles similar to glycosomes, containing enzymes of glycogenolysis. It is very likely that hydrolases in B. coli are formed on the rough reticular membranes without the involvement of cisterns of the Golgi complex. The ultrastructural deposits of the reaction to G-6-Pase and AlP in the trophozoites of B. coli described here indicate that some membranes of the rough endoplasmic reticulum and small vacuoles with a strong reaction to these enzymes can play a similar role to the Golgi complex.
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