Histochemical observations of alkaline phosphatase activity of Echinococcus multilocularis during in vivo development in golden hamsters, an alternative definitive host
Autor: | A F Petavy, M E Sarciron, S Walbaum, C Arsac |
---|---|
Rok vydání: | 1997 |
Předmět: |
Male
Prednisolone Foxes Echinococcus multilocularis General Biochemistry Genetics and Molecular Biology Microbiology In vivo Echinococcosis Cricetinae parasitic diseases Intestine Small medicine Animals General Veterinary biology Mesocricetus Histocytochemistry General Medicine Viral tegument biology.organism_classification Alkaline Phosphatase Small intestine Enzyme assay Echinococcus medicine.anatomical_structure Biochemistry Excretory system biology.protein Alkaline phosphatase Animal Science and Zoology Female Golden hamster |
Zdroj: | Experimental animals. 46(1) |
ISSN: | 1341-1357 |
Popis: | Histochemical observations of alkaline phosphatase activity of Echinococcus multilocularis during the in vivo development in golden hamster, an alternative definitive host. The present work reports on the ability of protoscoleces from a European fox strain of E. multilocularis to differentiate and develop into the adult form in the small intestine of male golden hamsters treated with prednisolone. Detection of alkaline phosphatase activity on various stages of the developing worm was performed by histochemical methods. The enzyme activity was not demonstrable in the early stages of infection but occurred with strobilization. Age-related changes in the distribution of the enzyme activity took place during strobilization. Alkaline phosphatase activity was evident in the excretory ducts of 8 to 11 day old strobila and in the tegument of mature proglottis of 16 day old worms. This in vivo procedure with rodents as definitive hosts provides interesting preliminary results on the biology of the E. multilocularis adult. Further investigations on membrane-bound enzymes involved in physiological and nutritional processes are in progress. |
Databáze: | OpenAIRE |
Externí odkaz: |